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J. Biochem, 1982, Vol. 92, No. 3 689-698
© 1982 Japanese Biochemical Society

research-article

Mechanism of Surface-Mediated Activation of Bovine Factor XII and Plasma Prekallikrein1,2

Teruko SUGO, Amélia HAMAGUCHI, Toshio SHIMADA, Hisao KATO and Sadaaki IWANAGA

Department of Biology, Faculty of Science, Kyushu University 33 Higashi-ku, Fukuoka, Fukuoka 812

The mechanism of kaolin-mediated activation of bovine Factor XII was studied in the presence of prekallikrein and HMW kininogen. The activated enzymes were assayed using fluorogenic peptide substrates, Boc-Glu(OBzl)-Gly-Arg-4-methyl-coumaryl-7-amide (MCA) for Factor XIIa and Z-Phe-Arg-MCA for plasma kallikrein. The rates of activation of the zymogens were separately measured by blocking either of the active enzymes with a specific inhibitor, corn inhibitor for Factor XIIa and Trasylol for plasma kallikrein. The results were as follows:

1. At the early stage of the activation reaction, kallikrein activity was first generated after a short lag phase, and then Factor XIIa activity was generated with a sigmoidal curve. In the presence of corn inhibitor, the activation of prekallikrein was observed, but in the presence of Trasylol, the activation of Factor XII was not observed. In the presence of a high concentration of Ala-Phe-Arg-CH2Cl, which immediately inactivates both of the active enzymes, the cleavage of a single chain prekallikrein into the two chain form by Factor XII was found, as revealed by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE), using nonlabeled and tritiated prekallikrein.

2. The incubation of Factor XII alone in a quartz cuvette or in the presence of kaolin and HMW kininogen did not result in the activation of Factor XII. The concave upward curve due to autocatalytic activation was not observed even after the addition of Factor XIIa to the Factor XII preparation. Moreover, no limited proteolysis of Factor XII during the incubation with kaolin and HMW kininogen was shown by SDS-PAGE, using 3H-Factor XII.

1 This study was supported by Grants-in-Aid (00543012 and 00587001) for Scientific Research from the Ministry of Education, Science and Culture of Japan and by a Yamada Research Grant for 1980.

2 Reported at the 54th annual meeting of the Japanese Biochemical Society held in Sendai (1981) Seikagaku (in Japanese) 53, 672.


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