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

Li      Li; Jing      Zhao; Rong-Qiao      He

doi:10.2174/0929866033479095

Abstract

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

« Previous Next »

Rights & Permissions Print Cite

Protein & Peptide Letters

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

Volume: 10 Issue: 2

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

Affiliation:

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

Abstract: 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.

Export Options

Export File:

RIS (for EndNote, Reference Manager, ProCite)

BibTeX

Text

Content:

Citation Only

Citation and Abstract

About this article

Cite this article as:

Li Li, Zhao Jing and He Rong-Qiao, Isolation And Some Characterizations Of A Glycosylated Fibrinolytic Enzyme Of Earthworm, Eisenia Fetida, Protein & Peptide Letters 2003; 10 (2) . https://dx.doi.org/10.2174/0929866033479095

DOI https://dx.doi.org/10.2174/0929866033479095	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305

About this journal

Call for Papers in Thematic Issues

Submission closes on : 01 February, 2025

Therapeutic Proteins and Peptides of Plant Origin

Plants are still the major repository of biologically active substances. In the last two decades, however, natural peptides and proteins of plant origin have gained increasing attention due to their pharmacological activities over a variety of human illness, including those mediated by infections and parasitosis and those involving different cellular ...read more

Guest Editor(s): Dr. Márcio Viana Ramos