Purification of granulin-like polypeptide from the blood-sucking leech, Hirudo nipponia.
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.
Hong
S J
SJ
Department of Biological Sciences, KAIST, Taejon, 305-701, Korea.
Kang
K W
KW
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D007865:Leeches; D008969:Molecular Sequence Data; D000077153:Progranulins; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000737:chemistry / Q000302:isolation & purification*
D036341:Intercellular Signaling Peptides and Proteins; D000077153:Progranulins; D014764:Viral Proteins