Search Results - (Author, Cooperation:W. Winckler)

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  1. 1
    Staff View
    Publication Date:
    2014-04-25
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    *Disease ; False Positive Reactions ; Genes/genetics ; Genetic Predisposition to Disease/*genetics ; Genetic Variation/*genetics ; *Guidelines as Topic ; Humans ; Information Dissemination ; Publishing ; Reproducibility of Results ; Research Design ; Translational Medical Research/standards
    Published by:
    http://www.nature.com/

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  2. 2
    Staff View
    Publication Date:
    2011-07-30
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Algorithms ; Apoptosis ; Carcinoma/*genetics/metabolism/virology ; Carcinoma, Squamous Cell ; Cell Differentiation ; Exons ; Head and Neck Neoplasms/*genetics/metabolism/virology ; Humans ; *Mutation ; Neoplasms, Squamous Cell/*genetics/metabolism/virology ; Papillomaviridae/isolation & purification ; Papillomavirus Infections/virology ; Point Mutation ; Receptor, Notch1/*genetics/metabolism ; *Sequence Analysis, DNA ; Sequence Deletion ; Signal Transduction ; Smoking ; Tobacco
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  3. 3
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    Publication Date:
    2011-03-25
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Amino Acid Sequence ; Blood Coagulation/genetics ; CpG Islands/genetics ; DNA Mutational Analysis ; DNA Repair/genetics ; Exons/genetics ; Exosome Multienzyme Ribonuclease Complex ; Genome, Human/*genetics ; Genomics ; Histones/metabolism ; Homeodomain Proteins/genetics ; Homeostasis/genetics ; Humans ; Methylation ; Models, Molecular ; Molecular Sequence Data ; Multiple Myeloma/drug therapy/enzymology/*genetics/metabolism ; Mutation/*genetics ; NF-kappa B/metabolism ; Oncogenes/genetics ; Open Reading Frames/genetics ; Protein Biosynthesis/genetics ; Protein Conformation ; Proto-Oncogene Proteins B-raf/antagonists & inhibitors/genetics/metabolism ; RNA Processing, Post-Transcriptional/genetics ; Ribonucleases/chemistry/genetics ; Signal Transduction/genetics ; Transcription, Genetic/genetics
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  4. 4
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    Publication Date:
    2011-02-11
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Carrier Proteins/genetics ; Case-Control Studies ; Cell Adhesion Molecules/genetics ; Chromatin/genetics/metabolism ; Chromosome Aberrations ; Chromosome Breakpoints ; Epigenesis, Genetic/genetics ; Gene Expression Regulation, Neoplastic ; Genome, Human/*genetics ; Humans ; Male ; PTEN Phosphohydrolase/genetics/metabolism ; Prostatic Neoplasms/*genetics ; Recombination, Genetic/genetics ; Signal Transduction/genetics ; Transcription, Genetic
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    http://www.nature.com/

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  5. 5
    J. Barretina ; G. Caponigro ; N. Stransky ; K. Venkatesan ; A. A. Margolin ; S. Kim ; C. J. Wilson ; J. Lehar ; G. V. Kryukov ; D. Sonkin ; A. Reddy ; M. Liu ; L. Murray ; M. F. Berger ; J. E. Monahan ; P. Morais ; J. Meltzer ; A. Korejwa ; J. Jane-Valbuena ; F. A. Mapa ; J. Thibault ; E. Bric-Furlong ; P. Raman ; A. Shipway ; I. H. Engels ; J. Cheng ; G. K. Yu ; J. Yu ; P. Aspesi, Jr. ; M. de Silva ; K. Jagtap ; M. D. Jones ; L. Wang ; C. Hatton ; E. Palescandolo ; S. Gupta ; S. Mahan ; C. Sougnez ; R. C. Onofrio ; T. Liefeld ; L. MacConaill ; W. Winckler ; M. Reich ; N. Li ; J. P. Mesirov ; S. B. Gabriel ; G. Getz ; K. Ardlie ; V. Chan ; V. E. Myer ; B. L. Weber ; J. Porter ; M. Warmuth ; P. Finan ; J. L. Harris ; M. Meyerson ; T. R. Golub ; M. P. Morrissey ; W. R. Sellers ; R. Schlegel ; L. A. Garraway
    Nature Publishing Group (NPG)
    Published 2012
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    Publication Date:
    2012-03-31
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Antineoplastic Agents/pharmacology ; Cell Line, Tumor ; Cell Lineage ; Chromosomes, Human/genetics ; Clinical Trials as Topic/methods ; *Databases, Factual ; Drug Screening Assays, Antitumor/*methods ; *Encyclopedias as Topic ; Gene Expression Profiling ; Gene Expression Regulation, Neoplastic ; Genes, ras/genetics ; Genome, Human/genetics ; Genomics ; Humans ; Mitogen-Activated Protein Kinase Kinases/antagonists & inhibitors/metabolism ; *Models, Biological ; Neoplasms/*drug therapy/genetics/metabolism/*pathology ; Pharmacogenetics ; Plasma Cells/cytology/drug effects/metabolism ; Precision Medicine/methods ; Receptor, IGF Type 1/antagonists & inhibitors/metabolism ; Receptors, Aryl Hydrocarbon/genetics/metabolism ; Sequence Analysis, DNA ; Topoisomerase Inhibitors/pharmacology
    Published by:
    http://www.nature.com/

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  6. 6
    Staff View
    Publication Date:
    2012-05-25
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Chromosome Breakpoints/radiation effects ; DNA Damage ; DNA Mutational Analysis ; Gene Expression Regulation, Neoplastic ; Genome, Human/*genetics ; Guanine Nucleotide Exchange Factors/*genetics/metabolism ; Humans ; Melanocytes/metabolism/pathology ; Melanoma/*genetics/pathology ; Mutagenesis/radiation effects ; Mutation/*genetics/radiation effects ; Oncogenes/genetics ; Sunlight/*adverse effects ; Ultraviolet Rays/adverse effects
    Published by:
    http://www.nature.com/

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  7. 7
    M. S. Lawrence ; P. Stojanov ; P. Polak ; G. V. Kryukov ; K. Cibulskis ; A. Sivachenko ; S. L. Carter ; C. Stewart ; C. H. Mermel ; S. A. Roberts ; A. Kiezun ; P. S. Hammerman ; A. McKenna ; Y. Drier ; L. Zou ; A. H. Ramos ; T. J. Pugh ; N. Stransky ; E. Helman ; J. Kim ; C. Sougnez ; L. Ambrogio ; E. Nickerson ; E. Shefler ; M. L. Cortes ; D. Auclair ; G. Saksena ; D. Voet ; M. Noble ; D. DiCara ; P. Lin ; L. Lichtenstein ; D. I. Heiman ; T. Fennell ; M. Imielinski ; B. Hernandez ; E. Hodis ; S. Baca ; A. M. Dulak ; J. Lohr ; D. A. Landau ; C. J. Wu ; J. Melendez-Zajgla ; A. Hidalgo-Miranda ; A. Koren ; S. A. McCarroll ; J. Mora ; R. S. Lee ; B. Crompton ; R. Onofrio ; M. Parkin ; W. Winckler ; K. Ardlie ; S. B. Gabriel ; C. W. Roberts ; J. A. Biegel ; K. Stegmaier ; A. J. Bass ; L. A. Garraway ; M. Meyerson ; T. R. Golub ; D. A. Gordenin ; S. Sunyaev ; E. S. Lander ; G. Getz
    Nature Publishing Group (NPG)
    Published 2013
    Staff View
    Publication Date:
    2013-06-19
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Artifacts ; DNA Replication Timing ; Exome/genetics ; False Positive Reactions ; Gene Expression ; *Genetic Heterogeneity ; Genome, Human/genetics ; Humans ; Lung Neoplasms/genetics ; Mutation/*genetics ; Mutation Rate ; Neoplasms/classification/*genetics/pathology ; Neoplasms, Squamous Cell/genetics ; Oncogenes/*genetics ; Reproducibility of Results ; Sample Size
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  8. 8
    Bohn, H. ; Winckler, W.
    Springer
    Published 1985
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Placental tissue proteins PP18, PP19, PP20, and PP21 ; Isolation ; Physical and chemical characterization ; Immunochemical quantitation
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary Four new soluble placental tissue proteins (PP18, PP19, PP20; PP21) have been isolated to purity from saline extracts of human term placentas. Two of the new proteins appear to be partly associated with placental membranes; they also could be detected in placental protein fractions obtained by extracting the insoluble part of the placental tissue with solubilizing agents after the soluble material had been removed by washing with saline. The new placental proteins were characterized by their physical properties as well as by their carbohydrate and aminoacid compositions. Specific antisera to the new proteins were obtained by immunizing animals with the corresponding purified proteins. They were used to detect and quantitate the new proteins in extracts of placentas and other human tissues by immunochemical methods. From one human term placenta an average of 2 mg PP18, 90 mg PP19, 0.5 mg PP20, and around 7 mg PP21 could be extracted. None of these new proteins is specific to the placenta; they also were found to occur in extracts of certain other human tissues. The immunohistochemical localization of these proteins as well as measurement of their concentrations in body fluids by sensitive radioimmunoassays are presently under investigation.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02133941

    Articles: DFG German National Licenses
  9. 9
    Bohn, H. ; Kraus, W. ; Winckler, W.
    Springer
    Published 1985
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Membrane-associated placental proteins ; Solubilisation ; Isolation ; Physico-chemical characterization ; Immunochemical quantitation
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary Two membrane associated placental tissue proteins (PP4 and MP1) have been isolated and characterized. Both proteins are found in the soluble as well as solubilized protein fractions of the human placenta and thus appear to be at least partly associated with placental membranes. PP4 has a molecular weight of 35000 and apparently consists of a single peptide chain. It has an electrophoretic mobility in between the α1- and α2-globulins, an isoelectric point of 4.85 and a sedimentation coefficient of 3.3 S. The carbohydrate content of PP4 amounts to 2.4%. MP1 was isolated from placental protein fractions solubilized with Triton X-100. It has a molecular weight of around 180000 and appears to be composed of two identical subunits which are non-covalently linked. MP1 was found to have an electrophoretic mobility in between the α2- and β1-globulins, an isoelectric point of 4.75 and a sedimentation coefficient of 6.65 S. MP1 is a glycoprotein which contains 9.6% carbohydrates. Immunochemical methods were used to detect and quantitate PP4 and MP1 in extracts of placentae and other human tissues. MP1 appears to be specific to the placenta, whereas PP4 was found to occur also in certain other human tissues. The diagnostic significance of detection and measurement of these proteins in tissues and body fluids is presently under investigation.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02133940

    Articles: DFG German National Licenses
  10. 10
    Bohn, H. ; Winckler, W.
    Springer
    Published 1977
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Placenta specific protein PP5 ; Isolation ; Physical and chemical characterization ; Protease inhibitor ; Placenta-spezifisches Protein PP5 ; Isolierung ; Physikalische und chemische Charakterisierung ; Proteaseinhibitor
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Description / Table of Contents:
    Zusammenfassung Beschrieben wird die Isolierung und Charakterisierung des Plazenta-Proteins PP5. Die Isolierung und Hochreinigung wurde mit Hilfe von Immunadsorbentien durchgeführt. Aus dem Gewebe einer ausgewachsenen menschlichen Plazenta (500 g) lassen sich im Durchschnitt etwa 15 mg dieses Proteins extrahieren. PP5 ist offensichtlich spezifisch für die Plazenta; im Extrakt von anderen menschlichen Organen konnte es nicht nachgewiesen werden. Im Serum schwangerer Frauen kommt PP5 nicht, oder höchstens in Spuren (〈0,1 mg%) vor. In der Ultrazentrifuge wurde für PP5 ein Sedimentationskoeffizient von 2,8 S und ein Molekulargewicht von 36 600 ermittelt. Die elektrophoretische Wanderung von PP5 entspricht der eines schnellenβ-Globulins. Der isoelektrische Punkt liegt bei pH 4,6. PP5 ist ein Glykoprotein und hat einen Kohlenhydratgehalt von 19,8% (Hexosen 10,0%, Hexosamin 4,4%, Fucose 0,4%, Neuraminsäure 5,0%). Die Aminosäurenzusammensetzung des Proteins wird ebenfalls mitgeteilt. PP5 inhibiert die Wirkung von Trypsin und Plasmin; seine biologische Funktion besteht möglicherweise in der Hemmung von Proteasen.
    Notes:
    Summary The isolation and characterization of placental protein PP5 is described. The purification was achieved by use of immunoadsorbents. From the tissue of one human term placenta an average amount of 15 mg PP5 can be extracted. PP5 apparently is specific for the placenta; it could not be detected in extracts from other human tissues. In sera from pregnant women PP5 is not present or only in trace amounts (〈0.1 mg%). In the ultracentrifuge PP5 was found to have a sedimentation coefficient of 2.8 S and a molecular weight of 36,600 daltons. Electrophoretically the protein migrates as a fastβ 1-globulin. The isoelectric point was determined to be 4.6. PP5 is a glycoprotein and contains 19.8% carbohydrates (hexoses 10.0%, hexosamine 4.4%, fucose 0.4%, sialic acid 5.0%). The amino acid composition of the protein is reported, too. PP5 was found to inhibit the activity of trypsin and plasmin; the biological role of this protein therefore may be the inhibition of proteases.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00667387

    Articles: DFG German National Licenses
  11. 11
    Bohn, H. ; Winckler, W.
    Springer
    Published 1987
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Placental protein 3 (PP3) ; Flavin (FAD)-containing protein ; Isolation ; Physico-chemical characterization ; Immunochemical quantitation
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary Placental protein 3 (PP3) has been isolated to purity from saline extracts of human term placentas. PP3 turned out to be a flavin-containing protein and thus appears to be an enzyme. The prosthetic group was identified as flavin-adenine dinucleotide (FAD) which was found to be noncovalently bound to the protein. The physical characterization of PP3 showed that the molecules are composed of two identical subunits having molecular weights of 55000 daltons which are noncovalently linked. Each subunit appears to contain one FAD group. In addition PP3 was found to have an electrophoretic mobility in between the α1 and α2 globulins, an isoelectric point in the range of 5.3–5.7, a sedimentation coefficient of 6.3 S and an extinction coefficient of 15.7 (E 1cm 1% 280 nm). Immunochemical methods were used to detect and quantitate PP3 in extracts of placentas and other human tissues. From one human term placenta an average of around 4 mg PP3 could be extracted; PP3 was also found to occur in extracts of adult human stomach. In concentrated extracts of other human tissues and in human body fluids this protein could not be detected, at least not in concentrations higher than 2 mg/dl.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02134068

    Articles: DFG German National Licenses
  12. 12
    Bohn, H. ; Winckler, W.
    Springer
    Published 1977
    Staff View
    ISSN:
    1432-0711
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Description / Table of Contents:
    Zusammenfassung Beschrieben wird die Isolierung und Charakterisierung eines neuen Gewebsproteins (PP7) aus dem Extrakt menschlicher Plazenten. Das Plazenta-Protein PP7 ist nicht spezifisch für die Plazenta; es kommt in relativ hoher Konzentration in praktisch allen Organen des Menschen vor. In Spuren ist es auch in Erythrozyten nachweisbar. In Seren konnte es weder mit dem Geldiffusionstest nach Ouchterlony noch mit der Elektroimmunodiffusionstechnik aufgefunden werden. PP7 hat ein Molekulargewicht von etwa 40 000 und ist offensichtlich aus zwei identischen Untereinheiten aufgebaut, die durch Nebenvalenzkräfte zusammengehalten werden. In der Ultrazentrifuge sedimentiert es mit 3,5 S. Bei der Elektrophorese wandert das Protein im Bereich zwischen denα 2- undβ 1-Globulinen. Sein isoelektrischer Punkt liegt bei 4,9. PP7 ist ein Glykoprotein und hat einen Kohlenhydratgehalt von 5,4% (Hexosen 3,0%, Hexosamine 1,2%, Fukose 0,2%, Neuraminsäure 1,0%). Die Aminosäurenzusammensetzung des Proteins wird ebenfalls mitgeteilt.
    Notes:
    Summary The isolation and characterization of a new tissue protein (PP7) from human placentae is described. The placental protein PP7 is not specific for the placenta; it is found in relative high concentrations in other human tissues as well. Trace amounts of PP7 occur in erythrocytes, too. In sera this protein could not be detected with the gel diffusion test of Ouchterlony nor with the electroimmunoassay technique. PP7 has a molecular weight of around 40,000 daltons and is composed of two identical subunits which are non-covalently linked. In the ultracentrifuge PP7 sediments with 3.5 S. The isoelectric point was found to be 4.9. Electrophoretically the protein migrates in the range betweenα 2 andβ 1-globulins. PP7 is a glycoprotein; its carbohydrate content amounts to 5.4% (hexoses 3.0%, Hexosamine 1.2%, Fucose 0.2%, sialic acid 1.0%). The amino acid composition of the protein is reported, too.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00670853

    Articles: DFG German National Licenses
  13. 13
    Bohn, H. ; Winckler, W.
    Springer
    Published 1980
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Placenta specific protein PP11 ; Isolation ; Physical and chemical characterization ; Immunochemical determination ; Plazentaspezifisches Protein PP11 ; Isolierung ; physikalische und chemische Charakterisierung ; immunchemische Bestimmung
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Description / Table of Contents:
    Zusammenfassung Beschrieben wird die Isolierung und Charakterisierung eines neuen Plazenta-Gewebsproteins (PP11) aus dem Extrakt reifer menschlicher Plazenten. Die Reinigung dieses Proteins erfolgte durch fraktionierte Fällung der Proteine mit Rivanol und Ammoniumsulfat sowie unter Verwendung der Gelfiltration und Ionenaustauschchromatographie und mit Hilfe von Immunadsorbentien. PP11 ist ein Glykoprotein und hat einen Kohlenhydratgehalt von 3,9% (Hexosen 2,6%, Hexosamine 1,0%, Fucose 0,05% und Neuraminsaure 0,26%). Auch die Aminosäurenzusammensetzung dieses Proteins wird mitgeteilt. PP11 hat die elektrophoretische Beweglichkeit eines α1-Globulins und einen Sedimentationskoeffizient von 3,5 S. In der Ultrazentrifuge wurde für das neue Protein ein Molekulargewicht von 44 300, im SDS-haltigen Polyacrylamidgel dagegen ein Molekulargewicht von 62 000 ermittelt. Der isoelektrische Punkt von PP11 liegt bei pH 5,1–5,2. Nachweis und Bestimmung von PP11 erfolgten mit immunologischen Methoden. Aus einer ausgewachsenen menschlichen Plazenta lassen sich im Durchschnitt 11 mg PP11 extrahieren. Im Extrakt anderer menschlicher Organe konnte das neue Protein nicht nachgewiesen werden; PP11 scheint demnach spezifisch für die Plazenta zu sein. In Seren und im Fruchtwasser kommt PP11 nicht oder nur in Spuren (〈 0,1 mg/100 ml) vor. Plazenten von Affen enthalten Proteine, die mit menschlichem PP11 immunchemisch identisch sind.
    Notes:
    Summary The isolation and characterization of a new placental protein (PP11) are described. The protein was purified from extracts of human term placentae by rivanol and ammonium sulfate fractionation, gel filtration, ion exchange chromatography, and by use of immunosorbents. PP11 is a glycoprotein which contains 3.9% carbohydrates (hexoses 2.6%, hexosamines 1.0%, fucose 0.05%, and sialic acid 0.26%). The amino acid composition of this protein was also determined. PP11 was found to have a sedimentation coefficient of 3.5 S, a molecular weight of 44,300 as determined in the ultracentrifuge and a molecular weight of 62,000 as determined by SDS-polyacrylamide gel electrophoresis. PP11 has the electrophoretic mobility of an α1 globulin and an isoelectric point at pH 5.1–5.2. For the detection and quantitation of PP11 immunochemical methods were used. From one human term placenta an average amount of 11 mg PP11 can be extracted. In extracts from other human tissues this protein could not be detected; it, therefore, appears to be specific to the placenta. PP11 was undetectable or present only in trace amounts (〈 0.1 mg/100 ml) in maternal and cord blood serum and in amniotic fluid. Placentae from monkeys contained proteins immunochemically identical to PP11.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02108580

    Articles: DFG German National Licenses
  14. 14
    Bohn, H. ; Winckler, W.
    Springer
    Published 1977
    Staff View
    ISSN:
    1432-0584
    Keywords:
    Hydroxyapatite-passing serum glycopro teins (HPG-1 and HPG-2) ; Human placental extract ; Physical and chemical properties ; Fibrinolytic activity ; Split product of coagulation factor XII ; Hydroxylapatit-passierende Globuline (HPG-1 und HPG-2) ; Extrakt menschlicher Plazenten ; Physikalische und chemische Eigenschaften ; Fibrinolytische Wirkung ; Spaltstück des Gerinnungsfaktors XII
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Description / Table of Contents:
    Zusammenfassung Beschrieben wird die Isolierung von zwei neuen, bisher offensichtlich noch nicht charakterisierten Serumproteinen aus dem Extrakt menschlicher Plazenten. Wegen ihrer Eigenschaft bei der Chromatographie an Hydroxylapatit in verdünnter Pufferlösung die Säule ungehindert zu passieren, werden sie als „Hydroxylapatit-passierende Globuline” (HPG-1 und HPG-2 bezeichnet.) HPG-1 ist ein Glykoprotein mit einem Kohlenhydratgehalt von 11,1%. Auf Azetatfolie wandert es elektrophoretisch zwischen Albumin und den α1Globulinen. HPG-1 hat einen Sedimentationskoeffizienten von 3,2 S. In der Ultrazentrifuge wurde für das Protein ein Molekulargewicht von 28 100 Daltons, im SDS-haltigen Polyakrylamidgel ein Molekulargewicht von 35 000 Daltons ermittel. Der isoelektrische Punkt von HPG-1 beträgt 4,3. Die Konzentration dieses Proteins im Serum liegt normalerweise zwischen 0–1 mg/100 ml. Bei Schwangerschaft und oraler Kontrazeption können die Werte auf das 2-bis Sfache ansteigen und liegen dann zwischen 0–3 mg/100 ml. HPG-2 ist ebenfalls ein Glykoprotein; es hat einen Kohlenhydratgehalt von 24,6%. Seine elektrophoretische Beweglichkeit liegt zwischen der von α1- und α2-Globulinen. HPG-2 sedimentiert mit 2,5 S. In der Ultrazentrifuge wurde für dieses Protein ein Molekulargewicht von 35 000 Daltons, im SDS-haltigen Polyakrylamidgel dagegen ein Molekulargewicht von 60–70 000 Daltons ermittelt. Der isoelektrische Punkt liegt bei 3,4. HPG-2 zeigt einen außergewöhnlich niedrigen Extinktionskoeffizienten (E 1cm 1% = 1,9); es wird daher vorgeschlagen, dieses Protein als low extinction oc-Glykoprotein zu bezeichnen. Die Konzentration von HPG-2 in Seren liegt normalerweise im Durchschnitt bei 15 mg/100 ml; etwas höhere Werte werden in Schwangerenseren (18,8mg%) und in Nabelschnurseren (17,4 mg%), etwas niedrigere Werte (II,2 mg%) bei Erkrankungen gefunden. HPG-2 läßt sich auch im Urin nachweisen; die Konzentration liegt dort im allgemeinen unter l mg/100 ml. Im Urin schwangerer Frauen steigen gegen Ende der Gravidität die Werte (maximal bis auf 2 mg/ 100 ml) an. Bei der Untersuchung auf enzymatische Aktivitäten wurde gefunden, daß HPG-1 eine proteolytische und fibrinolytische Wirkung besitzt. HPG-1 lagert sich im Serum an Antithrombin III an und ist aller Wahrscheinlichkeit nach ein Spaltstück des Gerinnungsfaktors XII (Hageman-Faktor). Die biologische Funktion von HPG-2 ist noch unbekannt.
    Notes:
    Summary The isolation of two new serum proteins from extracts of human placentae is described. Because of their properties to pass hydroxyapatite columns unhindred when applied in dilute buffer solutions these proteins are designated as hydroxyapatite-passing globulins (abbreviated to HPG-1 and HPG-2). HPG-1 is a glycoprotein containing 11.1% carbohydrates. Electrophoretically the protein migrates between albumin and α1globulins. HPG-1 sediments with 3.2 S. In the ultracentrifuge a molecular weight (MW) of 28,100 daltons and in SDS-PAA-gel electrophoresis a MW of 35,000 was determined. The isoelectric point was found to be 4.3, The concentration of HPG-1 in serum normally ranges from 1–2 mg/100 ml. In pregnant women and in oral contraceptive users serum levels may increase 2–3 fold, and then range from 0–3 mg/100 ml. HPG-2 is a glycoprotein, too. Its carbohydrate content amounts to 24.6%. Electrophoretically the protein migrates between α1- and α2-globulins. HPG-2 sediments with 2.5 S. In the ultracentrifuge a MW of 35,000 daltons, in SDS-PAA-gel electrophoresis a MW of 60,000–70,000 daltons was determined. The isoelectric point was found to be 3.4. HPG-2 shows an extraordinary low extinction coefficient (E 1cm 1% = 1.9); it is therefore proposed to designate this protein as low-extinction α-glycoprotein. The concentrations of HPG-2 in sera show a mean value of 15 mg/100 ml. Higher values are found in pregnancy sera (18.8 mg%) and in cord blood sera (17.4 mg%), lower values (11.2 mg%) in sera from diseased subjects. HPG-2 also can be detected in trace amounts (usually less than 1 mg%) in urine. In urine of pregnant women the concentration of HPG-2 increases in the last trimester and may reach levels as high as 2 mg/100 ml. HPG-1 was found to have proteolytic and fibrinolytic activity. In serum HPG-1 was shown to combine with antithrombin III. HPG-1 with all probability seems to be an active split product of coagulation factor XII (Hageman factor). The biological function of HPG-2 is still unknown.+
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00996143

    Articles: DFG German National Licenses
  15. 15
    Bohn, H. ; Winckler, W.
    Springer
    Published 1991
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Placental tissue proteins, PP22, PP23, PP24, PP25, and PP26 ; Isolation ; Physico-chemical characterization ; Immunochemical quantitation
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary Five new soluble placental tissue proteins (PP22, PP23, PP24, PP25, PP26) were isolated to purity from saline extracts of human term placentas and characterized by their physico-chemical properties. Specific antisera to the new proteins were obtained by immunizing animals with the corresponding purified proteins. They were used to detect and quantitate the new proteins in extracts of placentas and other human tissues by immunochemical methods such as gel diffusion tests. The immunhistochemical localization of the new proteins as well as measurement of their concentrations in body fluids by sensitive radioimmunoassays are presently under investigation.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02390087

    Articles: DFG German National Licenses
  16. 16
    Bohn, H. ; Winckler, W.
    Springer
    Published 1991
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Membrane-associated placental proteins MP2A, MP2B, MP2C, MP2D, MP2E, MP2F, MP2G, MP2H, MP2I, MP2K, MP2L, MP3, MP4, MP5, MP6, MP7, MP8, MP9 and MP10 ; Isolation ; Physico-chemical characterization ; Immunochemical quantitation
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary Membrane-associated proteins (MPS) of the human term placenta (afterbirth) were obtained by extracting the insoluble part of the tissue with solubilizing agents, after the soluble material had been removed by washing with saline. The insoluble residue was subsequently exhaustively extracted first with the nonionic detergent Triton X-100 and then with 6 M urea. In the Triton extract eleven new different membrane-associated antigens could be detected by immunochemical methods; they were designated as MP2A to MP2L. One of these proteins (MP2C) was found to be immunochemically identical with the already described soluble placental protein PP21 [3]. MP1 another antigen detected in the Triton extract later was identified as heat stable alkaline phosphatase. In the urea extract eight different membrane-associated antigens could be identified by immunochemical methods; they were designated as MP3 to MP10. MP3 later was found to be immunochemically identical with laminin. All these membrane-associated proteins have now been isolated to purity and characterized by their physico-chemical properties. Specific antisera to the new proteins were obtained by immunizing animals with the corresponding purified proteins. They were used to detect and quantitate the new proteins in extracts of placentas and other human tissues by immunochemical methods such as gel diffusion tests. The immunocytochemical localization of the new proteins as well as measurement of their concentrations in body fluids by sensitive radioimmunoassays or enzyme immunoassays are presently under investigation.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02390358

    Articles: DFG German National Licenses
  17. 17
    Bohn, H. ; Winckler, W. ; Grundmann, U.
    Springer
    Published 1991
    Staff View
    ISSN:
    1432-0711
    Keywords:
    Human placental proteins ; Immunochemical detection ; Biological functions ; Structural relationships
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary During the last 20 years a systematic search for proteins occurring in human term placenta (afterbirth) has been performed in our laboratory. As a result more than 30 soluble placental proteins and at least 20 different solubilized antigens apparently derived from the placental membranes have been identified by immunochemical methods in extracts from human term placentas. Most of these proteins have already been isolated to purity and characterized by their physicochemical parameters. Specific antisera to these proteins were obtained by immunizing animals with the corresponding purified proteins. They were used detect and localize these antigens by immunochemical methods in the placenta and in other human tissues. Sensitive immunochemical assays have been developed to exactly quantitate the new proteins in body fluids and to find out the diagnostic significance of measurement of these proteins in pregnant women and in patients with tumors and other diseases. Another aim was to elucidate the biological functions of our immunochemically detected proteins. The results obtained thus far are reported.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02391577

    Articles: DFG German National Licenses