Characterization of the particles of purified kappa-casein: trypsin as a probe of surface-accessible residues

kappa-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE. The disulfide-bonded caseins present range from dimer to octamer and above and preparations contain about 10% monomer. All of these heterogeneous polymers, however, self-associate in...

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Veröffentlicht in:	Journal of Protein Chemistry 1999-08, Vol.18 (6), p.637-652
Hauptverfasser:	Farrell, Jr, H M, Wickham, E D, Dower, H J, Piotrowski, E G, Hoagland, P D, Cooke, P H, Groves, M L
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Animals Biopolymers Casein Caseins - chemistry Caseins - isolation & purification Caseins - ultrastructure Cattle Chromatography, High Pressure Liquid Chymosin Cleavage Clusters Cow's milk Electron micrographs Electrophoresis, Polyacrylamide Gel Humans Kinetics Light scattering Liquid chromatography Microscopy, Electron Models, Molecular Molecular Probes Molecular Sequence Data Molecular weight Peptides pH effects Photon correlation spectroscopy Polymers Prediction models Protein Conformation Proteins Residues Sequence Homology, Amino Acid Substrates Surface Properties Three dimensional models Trypsin Trypsin - chemistry Ultracentrifugation
Online-Zugang:	Volltext
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