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The interaction of decorin core protein fragments with type I collagen.

Abstract：

:To further define the molecular interaction between decorin and type I collagen we generated a 20 kD fragment containing the N-terminal half of the core protein by Endoproteinase Arg C digestion and a 40 kD fragment including all leucine-rich repeats in the central part of decorin core by cleavage with 2-nitro-5-thiocyanobenzoate. The fragments did not influence collagen fibril formation, even at high concentration, and radioactive fragments showed little binding to collagen fibrils. Our observations suggest that neither the N-terminal half nor the central leucine-rich repeats of the decorin core protein can, by itself, interact fully with fibrillar collagen.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Pogány G,Vogel KG

doi

10.1016/0006-291x(92)91539-3

subject

Has Abstract

pub_date

1992-11-30 00:00:00

pages

165-72

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91539-3

journal_volume

189

pub_type

杂志文章

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