A fibrinolytic enzyme was isolated from a marine green alga, Codium latum,
and designated C. latum protease (CLP). It also had fibrinogenolytic activi
ty, hydrolyzing A alpha, B beta and gamma chains with preference in this or
der. As CLP hydrolyzed oxidized insulin B chain at position Arg(22)-Gly(23)
, and the peptide map of lysozyme digested with CLP was similar to that wit
h trypsin, CLP would be expected to have a high substrate specificity, simi
lar to that of trypsin. Protease activity peaked at pH 10, and was complete
ly inhibited by diisopropyl fluorophosphate (DFP). Therefore, we conclude t
hat CLP is a trypsin-like serine protease. (C) 1999 Elsevier Science Ltd. A
ll rights reserved.