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

Cited 33 time in webofscience Cited 0 time in scopus
  • Hit : 359
  • Download : 0
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 (pl 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. (C) 1999 Academic Press.
Publisher
ACADEMIC PRESS INC
Issue Date
1999-07
Language
English
Article Type
Article
Keywords

EPITHELIN PRECURSOR; GROWTH-FACTORS; PROTEINS; PEPTIDE; SEQUENCE; GENE; IDENTIFICATION; GIBBERELLIN; EXPRESSION; FAMILY

Citation

PROTEIN EXPRESSION AND PURIFICATION, v.16, no.2, pp.340 - 346

ISSN
1046-5928
URI
http://hdl.handle.net/10203/71407
Appears in Collection
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 33 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0