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Lipovitellin inhibition of Artemia trypsin-like proteinase: a role for a storage protein in regulating proteinase activity during development.

Abstract：

:Artemia trypsin-like proteinase has been reported previously to be highly inhibited in the embryo (B. Ezquieta and C.G. Vallejo (1985) Comp. Biochem. Physiol. 82B, 731-736). We report now that Artemia lipovitellin, the major storage protein complex, inhibits the proteinase. We have carried out an in vitro study of the characteristics of the inhibition. Lipovitellin, a glycolipoprotein of high molecular mass (650 kDa), behaves initially as a substrate but after a limited proteolysis becomes an inhibitor of the proteinase. The enzyme although inhibited in the hydrolysis of the protein substrate retains activity toward low molecular weight substrates. The residual activity on the protein substrate is inhibited by small inhibitors of the proteinase. These features of lipovitellin inhibition are reminiscent of the trap mechanism of alpha 2-macroglobulin inhibition, previously proposed as suitable for regulating proteolytic processes involved in development. Inhibition by lipovitellin is greater at low temperatures and has been determined at 17 and 37 degrees C, in the lower and higher part of the viable temperature range of Artemia development. At high temperature the proteinase hydrolyzes the inhibitor quite efficiently and the inhibition is lower. The inhibition by lipovitellin appears specific for Artemia trypsin-like proteinase when compared with other control pairs protein/proteinase. The results may provide support for an additional role of storage proteins as developmental inhibitors of proteinases.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Ezquieta B,Vallejo CG

doi

10.1016/0003-9861(86)90743-5

subject

Has Abstract

pub_date

1986-11-01 00:00:00

pages

410-7

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(86)90743-5

journal_volume

250

pub_type

杂志文章

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