| Literature DB >> 10643667 |
K Matsubara1, K Hori, Y Matsuura, K Miyazawa.
Abstract
A fibrinolytic enzyme was isolated from a marine green alga, Codium latum, and designated C. latum protease (CLP). It also had fibrinogenolytic activity, hydrolyzing A alpha, B beta and gamma chains with preference in this order. As CLP hydrolyzed oxidized insulin B chain at position Arg22-Gly23, and the peptide map of lysozyme digested with CLP was similar to that with trypsin, CLP would be expected to have a high substrate specificity, similar to that of trypsin. Protease activity peaked at pH 10, and was completely inhibited by diisopropyl fluorophosphate (DFP). Therefore, we conclude that CLP is a trypsin-like serine protease.Entities:
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Year: 1999 PMID: 10643667 DOI: 10.1016/s0031-9422(99)00356-8
Source DB: PubMed Journal: Phytochemistry ISSN: 0031-9422 Impact factor: 4.072