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. 1977 Jan 11;480(1):275-81.
doi: 10.1016/0005-2744(77)90340-0.

Kinetic studies of the urokinase catalysed conversion of NH2-terminal lysine plasminogen to plasmin

U Christensen, S Müllertz

Kinetic studies of the urokinase catalysed conversion of NH2-terminal lysine plasminogen to plasmin

U Christensen et al. Biochim Biophys Acta. .

Abstract

A method for determining initial velocities of the urokinase (EC 3.4.99.26) catalysed converstion of NH2-terminal lysine plasminogen to plasmin (EC 3.4.21.7) is presented. This reaction has been coupled with the hydrolysis of alpha-N-benzyoly-L-arginine ethyl ester, which is catalysed by plasmin, and its rate has been determined from the time course of the overall reaction. The proenzyme-enzyme conversion was found to obey the Michaelis-Menten rate equation. The following values of the kinetic parameters were obtained: the apparent Michaelis constant, Km = 40.7 +/- 6.2 muM; the catalytic constant, kc = 2.59+/-0.31 s(-1), and kc/Km = 6.36-10(4) +/- 0.24-10(4) M(-1)-s(-1).

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