title: A fibrinolytic enzyme from a marine green alga, Codium latum.
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.
authors.affiliation: Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University, Japan. kmatsuba@fhw.oka-pu.ac.jp
authors.forename: K
authors.initials: K
authors.lastname: Matsubara
authors.forename: K
authors.initials: K
authors.lastname: Hori
authors.forename: Y
authors.initials: Y
authors.lastname: Matsuura
authors.forename: K
authors.initials: K
authors.lastname: Miyazawa
mesh_terms: D000818:Animals; D002417:Cattle; D000460:Chlorophyta / Q000201:enzymology*; D004789:Enzyme Activation; D005340:Fibrinogen / Q000378:metabolism; D005342:Fibrinolysis; D005343:Fibrinolytic Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D010446:Peptide Fragments / Q000302:isolation & purification; D010449:Peptide Mapping; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D005343:Fibrinolytic Agents; D010446:Peptide Fragments; D005340:Fibrinogen; D012697:Serine Endopeptidases