Abstract
Plasminogen activator (PA) activity was demonstrated in a saline soluble fraction during middle and late stages of murine lepromas in high responder mice, C57BL/6NJcl. A single enzymatic peak at 23, 000 in molecular weight (MW) was detected with Sephacryl S-200gel chromatography. The enzyme fraction hydrolyzed 125I-fibrin only in the presence of plasminogen. The enzyme was found to be a trypsin-like serine proteinase in its substrate specificity and inhibitor spectrum.Furthermore, two distinct PA inhibitors were demonstrated in early lepromatous lesions. I1 (MW 82, 000) inactivated plasmin quickly and PA from lepromas slowly. I2 (MW 45, 000) showed time-dependent inhibition for PA from lepromas and urokinase.
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