期刊
JOURNAL OF ANTIBIOTICS
卷 53, 期 3, 页码 241-247出版社
JAPAN ANTIBIOT RES ASSN
DOI: 10.7164/antibiotics.53.241
关键词
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Two novel staplabin analogs, SMTP-7 and -8, have been isolated from cultures of Stachybotrys microspora IFO 30018. Spectroscopic analyses showed that the SMTP-7 molecule consisted of two identical staplabin core structures and ornithine which bridges the two partial structures. In the SMTP-8 molecule, the bridging unit was lysine. At concentrations of 80 similar to 150 mu M, the two compounds caused 2- to 12-fold increase in urokinase-catalyzed plasminogen activation, fibrin binding of plasminogen, and urokinase- and plasminogen-mediated fibrinolysis. These activities of SMTP-7 and -8 were two to ten times higher than those of staplabin and previously isolated SMTPs. which exerted such effects at concentrations ranging from 150 to 800 mu M.
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