:Comparative study of fibrin-binding and thrombolytic properties with those of the intact and degraded molecular forms of urokinase

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• The fibrin-binding and thrombolytic properties of high molecular weight urokinase with a single polypeptide chain (single-chain HMW-UK) and of other molecular forms of urokinase were compared. The single-chain HMW-UK (mol. wt. 53, 400; 61, 800IU/mg protein) was highly purified from human kidney tissue cultures by affinity chromatography on [Nα-(ε-aminocaproyl)-DL-homoar- ginine hexylester]-Sepharose, isoelectric focusing, and gel filtration on Sephadex G-100. In contrast to the similarity in amidase activity (Km 92-106μM, kcat 28-31s-1; kcat/Km=0.27-0.34μM-1s-1) and Glu-plasminogen activation (Kplg0.63-0.90μM, kplg28-29min-1; kplg/Kplg=32-45μM-1min-1) of the singlechain HMW-UK and HMW-UK (urinary source, composed of two polypeptide chains; mol. wt. 53, 000 124, 000IU/mg protein), the fibrin-binding affinity was different. Using a fibrin-Sepharose column, it was found that the single-chain HMW-UK had a much higher affinity towards the fibrin molecule than HMWUK, LMW-UK (urinary source; mol. wt. 31, 500, 230, 000IU/mg protein), LMWtryp-UK (trypsin digested form of HMW-UK; mol. wt. 36, 000, 101, 000IU/mg protein) or active H-chain (functionally-active heavy chain of HMW-UK; mol. wt. 31, 000, 208, 000IU/mg protein). The main activity peak of the single-chain HMW-UK was eluted at an NaCl concentration exceeding 0.5M. The light chain part of the single-chain HMW-UK was thought to include the fibrin-binding site, in contrast to the heavy chain part being proved to contain the active site. After intravenous injection of single-chain HMW-UK (3, 000IU/kg) in cases of experimental dog thrombus, strong activation of plasma fibrinolysis was observed.Furthermore, a much higher thrombolytic effect with single-chain HMW-UK was confirmed from X-ray micrographs.

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一般社団法人 日本血栓止血学会 | 論文

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