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Evidence for multiple interacting binding sites in bovine tryptase.

Abstract：

:The interaction of bovine pancreatic trypsin inhibitor (BPTI) and bovine tryptase, which are co-localized in the same granules of bovine mast cells, has been analyzed at 30 degrees C in 0.1 M Tris-HCl, pH 8.0. The analysis has unravelled that the functional unit of bovine tryptase is formed of (at least) four binding sites for this inhibitor. These interaction sites display a simple binding behaviour for small inhibitors (and substrates), whereas heterogeneous properties have been observed in the binding of BPTI. Furthermore, in the presence of BPTI, a positive functional interaction can be detected among the binding sites also for a small synthetic inhibitor, like benzamidine. Such features indicate the existence of a complex functional interplay among the sites of the functional unit which is transmitted through the secondary specificity sites.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fiorucci L,Erba F,Coletta M,Ascoli F

doi

10.1016/0014-5793(95)00286-i

subject

Has Abstract

pub_date

1995-04-17 00:00:00

pages

81-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00286-I

journal_volume

363

pub_type

杂志文章

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