| Literature DB >> 15604774 |
Xue-Ming Tang1, F M Lakay, Wei Shen, Wei-Lan Shao, Hui-Ying Fang, B A Prior, Zheng-Xiang Wang, Jian Zhuge.
Abstract
An extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at 60 degrees C (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition.Entities:
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Year: 2004 PMID: 15604774 DOI: 10.1023/B:BILE.0000045642.19299.3f
Source DB: PubMed Journal: Biotechnol Lett ISSN: 0141-5492 Impact factor: 2.461