Purification and molecular cloning of a novel serine protease from the centipede, Scolopendra subspinipes mutilans.

Abstract:

:A novel serine protease, named as scolonase, was purified and characterized from the tissue of the Korean centipede, Scolopendra subspinipes mutilans. Purified scolonase showed an apparent molecular weight of 25 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and an isoelectric point of 4.8 on isoelectric focusing gel. Scolonase was able to preferentially hydrolyze arginine over lysine at the cleavage site among the several synthetic peptide substrates. Scolonase has also a potent fibrinolytic activity by converting human Glu-plasminogen to activated plasmin due to the specific cleavage of the molecule at the peptide bond Arg(561)-Val(562). The enzyme activity of scolonase was completely inhibited by phenylmethanesulfonyl fluoride and difluorophosphate. The cDNA encoding scolonase was cloned from the cDNA library of the centipede constructed with oligonucleotide probe, which was designed on the basis of the N-terminal amino acid sequence of scolonase. The deduced complete amino acid sequence of scolonase demonstrated that the protein is composed of 277 amino acids including 33 amino acids as a leader sequence, and that it has significant sequence homology with other serine proteases.

authors

You WK,Sohn YD,Kim KY,Park DH,Jang Y,Chung KH

doi

10.1016/j.ibmb.2003.10.003

subject

Has Abstract

pub_date

2004-03-01 00:00:00

pages

239-50

issue

3

eissn

0965-1748

issn

1879-0240

pii

S0965174803001954

journal_volume

34

pub_type

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