Bovine renal cortex type I collagen: high contents of 3- and 4-hydroxyprolines.
Type I collagen was prepared from bovine renal cortices by pepsin digestion followed by differential salt fractionation, and was identified by SDS-polyacrylamide gel electrophoresis, CM-cellulose chromatography, and by the analysis of CNBr-cleavage products of the alpha 1 chain. About 61-87% of total collagen in the tissue was solubilized by this procedure and type I collagen represents about 40% of the collagen solubilized. Renal cortex type I collagen is characteristic in that the extent of hydroxylation of the prolyl residues is high, but that of the lysyl residues is at the same level as in skin. Tissue-specific differences in the hydroxylation of prolyl residues of type I collagen are also discussed.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003094:Collagen / Q000032:analysis*; D003488:Cyanogen Bromide; D006901:Hydroxylysine / Q000032:analysis; D006909:Hydroxyproline / Q000032:analysis*; D007672:Kidney Cortex / Q000032:analysis*; D012867:Skin / Q000032:analysis
D000596:Amino Acids; D006901:Hydroxylysine; C026215:3-hydroxyproline; D003094:Collagen; D003488:Cyanogen Bromide; D006909:Hydroxyproline