| Literature DB >> 15973058 |
Matsujiro Ishibashi1, Sayaka Yamashita, Masao Tokunaga.
Abstract
A halophilic alkaline phosphatase was highly purified (about 510-fold with about 21% yield) from a moderate halophile, Halomonas sp. 593. The N-terminal 35 amino acid sequence of this enzyme was found to be more acidic than those previously isolated from Vibrio spp., and this enzyme was partially resistant to SDS. Several enzymatic properties demonstrated that it showed higher halophilicity than those enzymes from Vibrio spp.Entities:
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Year: 2005 PMID: 15973058 DOI: 10.1271/bbb.69.1213
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043