Open AccessStructure of human‐basement‐membrane (type IV) collagen
Author(s) -
BABEL Wilfred,
GLANVILLE Robert W.
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08404.x
Subject(s) - basement membrane , type iv collagen , basement , type (biology) , chemistry , biophysics , microbiology and biotechnology , geology , biology , laminin , extracellular matrix , biochemistry , geography , paleontology , archaeology
The complete amino acid sequence of the 914‐residue‐long pepsin fragment α1(IV)95 from the α1 chain of human placental basement membrane (type IV) collagen is presented. This sequence contains 12 interruptions of the collagenous triplet sequence Gly‐Xaa‐Yaa which varied in length from 1 to 11 residues. The distribution of amino acids between the Xaa and Yaa position was similar to that found in interstitial collagens but the extent of proline and lysine hydroxylation differed. Computer comparisons of the α1(IV)95 sequence with those of the interstitial collagen chains did not reveal any homology, whereas a comparison with the partial sequences of mouse tumor and bovine lens capsule α1(IV) showed an approximately 85% identity. The unique sequence characteristics of type IV collagen are discussed in relation to its macromolecular structure and to the interstitial collagens.