Search Results - (Author, Cooperation:M. J. Weise)
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1B. A. Block ; I. D. Jonsen ; S. J. Jorgensen ; A. J. Winship ; S. A. Shaffer ; S. J. Bograd ; E. L. Hazen ; D. G. Foley ; G. A. Breed ; A. L. Harrison ; J. E. Ganong ; A. Swithenbank ; M. Castleton ; H. Dewar ; B. R. Mate ; G. L. Shillinger ; K. M. Schaefer ; S. R. Benson ; M. J. Weise ; R. W. Henry ; D. P. Costa
Nature Publishing Group (NPG)
Published 2011Staff ViewPublication Date: 2011-06-24Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Animal Identification Systems ; Animal Migration ; Animals ; Aquatic Organisms/*physiology ; Bayes Theorem ; Biodiversity ; California ; Climate ; *Ecosystem ; Locomotion/*physiology ; North America ; Pacific Ocean ; Population Dynamics ; Predatory Behavior/*physiology ; Seasons ; Species Specificity ; Water Movements ; WildernessPublished by: -
2Greenfield, S. ; Weise, M. J. ; Gantt, G. ; Hogan, E. L. ; Brostoff, S. W.
Oxford, UK : Blackwell Publishing Ltd
Published 1982Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Proteins in peripheral nervous system and central nervous system myelin and homogenates of sciatic nerve and brain from young and adult mice and rats were characterized with affinity-purified anti-P2 and anti-myelin basic protein sera after electrophoretic transfer from sodium dodecyl sulfate-polyacrylamide gels to nitrocellulose sheets. Using this method we have identified a component of rodent peripheral nervous system myelin as P2 protein. Peripheral nervous system myelin also showed the presence of four basic proteins in addition to P2 protein. These were found to be analogous to the 14, 17, 18.5, and 21.5K species found in the central nervous system myelin. A number of high-molecular-weight proteins were also detected with anti-myelin basic protein serum in peripheral nervous system, as well as central nervous system myelin. In addition, we report the presence of a high-molecular-weight P2 cross-reactive protein in rodent brain stem homogenates, but not in central nervous system myelin.Type of Medium: Electronic ResourceURL: -
3Staff View
ISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Circular dichroism (CD) was used to study the conformations of bovine nerve root P2 basic protein, its reduced and carboxymethylated derivative (RCM-P2), and its large cyanogen bromide fragment (CN1). Data in the far UV show that both the parent protein and RCM-P2 have conformations dominated by a large amount of β structure. However, the CN1 peptide appears to exist in a largely unordered conformation. Since CN1 lacks short (20 residue) amino- and carboxy-terminal segments of the P2 protein, the spectral data suggest that these regions are important for determining and/or maintaining folding of the P2 protein in aqueous solutions. The P2 protein was found to have a distinctive CD spectrum in the near UV. The characteristics of molar ellipticities indicate that the spectrum contains significant contributions from tyrosine residues, and that these contributions suggest different environments for the two tyrosines in P2 protein. Both environments depend on protein conformation, since CD side chain absorptions are lost when P2 protein is denatured with 5 M urea.Type of Medium: Electronic ResourceURL: -
4Weise, M. J. ; Hsieh, D. ; Hoffman, P. M. ; Powers, J. M. ; Brostoff, S. W.
Oxford, UK : Blackwell Publishing Ltd
Published 1980Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Cleavage of bovine P2 protein by cyanogen bromide (CNBr) produced peptide fractions CN1, CN2, and CN3 which were isolated by gel filtration chromatography. CN2 was found to contain two NH2-terminals (lysine and valine) and accounted for both of the cysteine residues of P2. When reduced carboxymethylated P2 (RCM-P2) was digested with CNBr, peptides CN1 and CN3 were obtained as were (1) a peptide with NH2-terminal lysine (Lys) that contained no homoserine and only one cysteine residue and (2) a peptide with NH-2-terminal valine (Val) that was co-eluted with CN3. These data and the chemical characterization of all the CNBr peptides obtained from P2 and RCM-P2 suggest that isolated P2 protein has a structure composed of the CNBr peptides in the order CN3-CN1-CN2(Val)-CN2(Lys) with an intrachain disulfide bond between the cysteine residues located in the two constituent peptides of CN2, CN2(Lys) and CN2(Val), To locate the neuritogenic region(s) within the P2 protein structure, CN1, CN2, and CN3 were tested for the ability to induce experimental allergic neuritis (EAN) in Lewis rats. The disease-inducing sites of P2 protein were found only in CN1; neither CN2 nor CN3 produced disease. EAN induced by CN1 was comparable to that induced with P2 protein as determined by disease onset, clinical symptoms, and histologic lesions.Type of Medium: Electronic ResourceURL: -
5Hsieh, D. L. ; Weise, M. J. ; Levit, S. ; Powers, J. M. ; Brostoff, S. W.
Oxford, UK : Blackwell Publishing Ltd
Published 1981Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: The sequence of the carboxyterminal 18 amino acids released by cyanogen bromide digestion of the bovine P2 protein was determined. It has several interesting structural and immunological properties. It contains the only two half-cystines in the molecule that have the capacity to form an intrachain disulfide bond. Using the rabbit as a test animal, this carboxyterminal peptide was capable of producing experimental allergic neuritis. The sequence of this peptide is Val-Val-Glu-Cys-Lys-Met-Lys-Asp-Val-Val-Cys-Thr-Arg-Ile-Tyr-Glu-Lys-Val.Type of Medium: Electronic ResourceURL: -
6Staff View
ISSN: 1432-1424Source: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Summary Self-exchange of chloride and sulfate in dog and cat red cells has been measured under equilibrium conditions. The rates of efflux for these anions are approximately twofold higher in dog compared to cat red blood cells. Although the rates differ, the anion exchange systems of these two red cell types exhibit many common properties. The dependence of35SO4 efflux on the intracellular SO4 concentration, the pH dependence and the inhibition of35SO4 efflux by Cl and SITS are almost identical in dog and cat red cells. Nystatin treatment was used to study the dependence of36Cl efflux on internal Cl. Chloride efflux exhibits saturation in both cell types with dog red cells possessing a higherV max andK 1/2 than cat red cells. The number of anion transport sites was estimated by extrapolation to the number of molecules of dihydro DIDS (H2DIDS, where DIDS is 4,4′-diisothiocyano-2,2′ stilbene-disulfonic acid) which were bound at 100% inhibition of transport. The results indicate that either the turnover numbers for anion transport differ in dog, cat, and human red cells or that there is heterogeneity in the function of the membrane components which bind H2DIDS.Type of Medium: Electronic ResourceURL: