Purification of granulin-like polypeptide from the blood-sucking leech, Hirudo nipponia.

Abstract:

:A cysteine-rich (approximately 20%), low molecular weight (MW 6 kDa) polypeptide has been isolated from the Korean blood-sucking leech, Hirudo nipponia. From its amino acid composition and N-terminal amino acid sequence analysis, the new protein is similar to granulin (or epithelin), and so it has been named leech granulin. The leech granulin behaved as a thrombin inhibitor in the purification steps of size-exclusion, ion-exchange, chromatofocusing, and reverse-phase high-performance liquid chromatography. The leech granulin is an acidic peptide (pI 3.75) containing high cysteine residues with a unique sequence similar to granulins or epithelins isolated from other organisms. For the first time, a granulin-like polypeptide having thrombin inhibitory activity has been isolated from a leech species.

journal_name

Protein Expr Purif

authors

Hong SJ,Kang KW

doi

10.1006/prep.1999.1077

keywords:

subject

Has Abstract

pub_date

1999-07-01 00:00:00

pages

340-6

issue

2

eissn

1046-5928

issn

1096-0279

pii

S104659289991077X

journal_volume

16

pub_type

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