Sequence comparison of pepsin-resistant segments of basement-membrane collagen alpha 1(IV) chains from bovine lens capsule and mouse tumour.
The C-terminal peptic fragment P1 (about 518 amino acid residues) of bovine lens-capsule collagen alpha 1(IV) chain was cleaved with CNBr and trypsin. The peptides were purified and characterized, allowing their ordering within the P1 fragment by comparison with a corresponding section of mouse collagen alpha 1(IV) chain [Schuppan, Glanville & Timpl (1982) Eur. J. Biochem. 123, 505-512]. About 67% of the sequence of bovine collagen fragment P1 was determined by Edman degradation. Comparison with the sequence of the corresponding mouse collagen fragment P1 showed 76% identity for positions Xaa and Yaa of the triplet structures Gly-Xaa-Yaa. Invariance was found for the positions of two non-triplet interruptions and of 3-hydroxyproline residues, pointing to the functional importance of these structures.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003094:Collagen; D003488:Cyanogen Bromide; D007903:Lens Capsule, Crystalline / Q000032:analysis*; D007908:Lens, Crystalline / Q000032:analysis*; D051379:Mice; D010434:Pepsin A; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D010446:Peptide Fragments; D003094:Collagen; D014357:Trypsin; D010434:Pepsin A; D003488:Cyanogen Bromide