The binding of heparin to type IV collagen: domain specificity with identification of peptide sequences from the α1(IV) and α2(IV) which preferentially bind heparin-Reference-Cited by-同舟云学术

The binding of heparin to type IV collagen: domain specificity with identification of peptide sequences from the α1(IV) and α2(IV) which preferentially bind heparin

Published:1989-02 Issue:4 Volume:264 Page:2313-2323
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Koliakos G G,Kouzi-Koliakos K,Furcht L T,Reger L A,Tsilibary E C

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference41 articles.

1. Structure of human-basement-membrane (type IV) collagen. Complete amino-acid sequence of a 914-residue-long pepsin fragment from the alpha1(IV) chain

2. Structure of the amino-terminal portion of the murine alpha 1(IV) collagen chain and the corresponding region of the gene.

3. Human basement membrane collagen (type IV). The amino acid sequence of the alpha2(IV) chain and its comparison with the alpha1(IV) chain reveals deletions in the alpha1(IV) chain

4. Construction of a model for the aggregation and cross-linking region (7S domain) of type IV collagen based upon an evaluation of the primary structure of the alpha1 and alpha2 chains in this region

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