作者: B. Caterson , J.R. Baker , D. Levitt , J.W. Paslay
DOI: 10.1016/S0021-9258(19)83526-3
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摘要: Link proteins from bovine nasal cartilage have been purified by preparative polyacrylamide gel electrophoresis in sodium dodecyl sulfate (Baker, J.R., and Caterson, B. (1979) J. Biol. Chem. 254, 2387-2393) used to raise antisera rabbits. A sensitive radioimmunoassay procedure utilizing binding of 125I-labeled antigen . antibody complexes Protein Staphylococcus aureus has served demonstrate the specificity for link proteins. The lack reactivity with proteoglycan fractions indicates that do not share antigenic determinants. This result is accord published cyanogen bromide peptide cleavage data Caterson (1977) Biochem. Biophys. Res. Commun. 77, 1-10) which showed protein be structurally dissimilar. quantitate small amounts remain associated after purification equilibrium density gradient centrifugation 4 M guanidine HCl chromatography sulfate.