Low molecular weight serine protease inhibitors from insects are proteins with highly conserved sequences.

Abstract:

:A low molecular weight protease inhibitor peptide found in ovaries of the desert locust Schistocerca gregaria (SGPI-2), was purified from plasma of the same locust and sequenced. It was named SGCI. It was found active towards chymotrypsin and human leukocyte elastase. SGCI was synthesized using a solid-phase procedure and the sequence of its reactive site for chymotrypsin was determined. Compared with an inhibitor purified earlier from another locust species, the total sequence of SGCI showed 88% identity. In particular, the sequence of the reactive site of these inhibitors was identical. Our search for a closely related peptide in an insect species far removed from locusts, the lepidopteran Spodoptera littoralis, was unfruitful but a different chymotrypsin inhibitor, belonging to the Kazal family, was found whose mass is greater than that of SGCI (20 vs 3.6 kDa). Its N-terminal sequence shares 80% identity with that of a chymotrypsin inhibitor purified earlier from the haemolymph of another lepidopteran. Conservation of the amino acid sequence in the reactive site seems to be an exception among protease inhibitors.

authors

Boigegrain RA,Pugnière M,Paroutaud P,Castro B,Brehélin M

doi

10.1016/s0965-1748(99)00109-5

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

145-52

issue

2

eissn

0965-1748

issn

1879-0240

pii

S0965174899001095

journal_volume

30

pub_type

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