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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Isolation And Some Characterizations Of A Glycosylated Fibrinolytic Enzyme Of Earthworm, Eisenia Fetida

Author(s): Li Li, Jing Zhao and Rong-Qiao He

Volume 10, Issue 2, 2003

Page: [183 - 190] Pages: 8

DOI: 10.2174/0929866033479095

Price: $65


Resin coupled with m-aminophenylbornic acid was used to isolate a glycosylated component from homogenate of earthworm (Eisenia fetida). The fraction showed a single band on SDS-PAGE with a molecular weight of 34,193 Da determined by mass spectroscopy. The N-terminal region is AQVCCPDI, different from those of earthworm fibrinolytic enzymes reported previously (Nakajima et al. 1993). This glycosylated component showed an activity on digesting both Chromozym-TH and fibrin, suggesting that it is a novel fibrinolytic enzyme.

Keywords: earthworm fibrinolytic enzyme, glycosylated earthworm fibrinolytic enzyme, isolation, chromozym-th, affinity chromatography

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