| Literature DB >> 15104136 |
Yong-Kee Jeong1, Woong Suk Yang, Kwang Hyuk Kim, Kyung Tae Chung, Woo Hong Joo, Jae Hyun Kim, Dong-Eun Kim, Jeong Uck Park.
Abstract
A fibrinolytic enzyme, myulchikinase, from a Korean seasoning ingredient, myul-chi-jeot-gal, has been purified to electrophoretic homogeneity. The molecular mass of the myulchikinase was estimated to about 28 kDa by SDS-PAGE and gel filtration. Amino acid sequence of the NH2-terminal of myulchikinase showed significant homology with other fibrinolytic enzymes including trypsin from starfish, katsuwokinase, and rat pancreatic elastase II. The purified myulchikinase hydrolyzed various synthetic substrates with different substrate specificity and cytotoxic to the tumor cell lines.Entities:
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Year: 2004 PMID: 15104136 DOI: 10.1023/b:bile.0000018257.18617.6d
Source DB: PubMed Journal: Biotechnol Lett ISSN: 0141-5492 Impact factor: 2.461