Sequence comparison of pepsin-resistant segments of basement-membrane collagen α1(IV) chains from bovine lens capsule and mouse tumor

D. Schuppan, R. W. Glanville, R. Timpl, S. N. Dixit, Andrew Kang

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The C-terminal peptic fragment P1 (about 518 amino acid residues) of bovine lens-capsule collagen α1(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 α1(IV) chain. 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% identify 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.

Original languageEnglish (US)
Pages (from-to)227-233
Number of pages7
JournalBiochemical Journal
Volume220
Issue number1
DOIs
StatePublished - Jan 1 1984

Fingerprint

Pepsin A
Basement Membrane
Lenses
Capsules
Tumors
Collagen
Neoplasms
Invariance
Trypsin
Digestion
Amino Acids
Degradation
Peptides

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Sequence comparison of pepsin-resistant segments of basement-membrane collagen α1(IV) chains from bovine lens capsule and mouse tumor. / Schuppan, D.; Glanville, R. W.; Timpl, R.; Dixit, S. N.; Kang, Andrew.

In: Biochemical Journal, Vol. 220, No. 1, 01.01.1984, p. 227-233.

Research output: Contribution to journalArticle

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