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Expression, purification and functional characterisation of a Kunitz-type module from chicken type VI collagen.

Abstract：

:The primary amino acid sequence of the carboxyl-terminal portion of the alpha 3 chain of chicken type VI collagen (K-VI) presents a 58-residue motif with a high degree of homology with members of the Kunitz serine-proteinase inhibitors family. This module was cloned, expressed in E. coli, purified and compared to the bovine pancreatic trypsin inhibitor (BPTI) in an inhibition profile assay of two serine proteases, trypsin and plasmin. We found that recombinant K-VI is not endowed with inhibitory activity but it slightly activates both plasmin and trypsin, differently from other members of the family. Moreover, the ability to inhibit the serine protease activity is also lacking in the intact type VI collagen molecule.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bearz A,Tolazzi G,Leonardi A,Pucillo C,Tell G,Colombatti A,Formisano S

doi

10.1006/bbrc.1995.2570

subject

Has Abstract

pub_date

1995-10-24 00:00:00

pages

1050-5

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X85725703

journal_volume

215

pub_type

杂志文章

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