Search Results - (Author, Cooperation:B. O'Dowd)
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1C. Nguyen ; R. W. Haushalter ; D. J. Lee ; P. R. Markwick ; J. Bruegger ; G. Caldara-Festin ; K. Finzel ; D. R. Jackson ; F. Ishikawa ; B. O'Dowd ; J. A. McCammon ; S. J. Opella ; S. C. Tsai ; M. D. Burkart
Nature Publishing Group (NPG)
Published 2013Staff ViewPublication Date: 2013-12-24Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Acyl Carrier Protein/*chemistry/*metabolism ; Binding Sites ; Catalytic Domain ; Cross-Linking Reagents/chemistry ; Crystallography, X-Ray ; Escherichia coli/*chemistry ; Fatty Acid Synthase, Type II/chemistry/metabolism ; Fatty Acids/*biosynthesis ; Histidine/metabolism ; Hydro-Lyases/chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Dynamics Simulation ; Protein Binding ; Protein Interaction MapsPublished by: -
2Staff View
ISSN: 1573-4935Source: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract The subunit structures of placental Hex A and B have previously been assigned as βa and βb, respectively. The β2 subunit is composed of two non-identical polypeptide chains, βa and βb. Purified Hex A and B were fractionated on a chromatofocusing column, and the fractions were reduced and then alkylated with iodo-I-14C-acetamide. The polypeptide chains were separated by polyacrylamide-gel isoelectric focusing. From the radioactivity measurements of the polypeptides a constant value for β2 was obtained in all the chromatofocusing fractions, demonstrating a non-random structure of (β2) in each β2 subunit.Type of Medium: Electronic ResourceURL: