Structure of human-basement-membrane (type IV) collagen. Complete amino-acid sequence of a 914-residue-long pepsin fragment from the alpha 1(IV) chain

Eur J Biochem. 1984 Sep 17;143(3):545-56. doi: 10.1111/j.1432-1033.1984.tb08404.x.


The complete amino acid sequence of the 914-residue-long pepsin fragment alpha 1 (IV)95 from the alpha 1 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 alpha 1 (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 alpha 1 (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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Basement Membrane / analysis*
  • Chemical Phenomena
  • Chemistry
  • Chromatography / methods
  • Collagen*
  • Cyanogen Bromide
  • Humans
  • Pepsin A
  • Peptide Fragments / isolation & purification*
  • Placenta / analysis


  • Peptide Fragments
  • Collagen
  • Pepsin A
  • Cyanogen Bromide