TY - JOUR
T1 - The hydrolysis of α-CBZ-l-lysine-p-nitrophenyl ester by two forms of human urokinase
AU - Ascenzi, Paolo
AU - Bertollini, Alberto
AU - Verzili, Daniela
AU - Brunori, Maurizio
AU - Antonini, Eraldo
PY - 1980/3/15
Y1 - 1980/3/15
N2 - The catalytic properties of human urokinase have been investigated using a synthetic chromogenic substrate; α-CBZ-l-lysine-p-nitrophenyl ester (ZLNP). The enzymatic assay based on the rate of hydrolysis of ZLNP offers several advantages over other methods currently employed in different laboratories. The steady state parameters of the two purified forms of human urokinase, which differ in molecular weight (33,000 and 54,000 daltons), have been determined over the pH range 5.2-7.8, and found to be indistinguishable.
AB - The catalytic properties of human urokinase have been investigated using a synthetic chromogenic substrate; α-CBZ-l-lysine-p-nitrophenyl ester (ZLNP). The enzymatic assay based on the rate of hydrolysis of ZLNP offers several advantages over other methods currently employed in different laboratories. The steady state parameters of the two purified forms of human urokinase, which differ in molecular weight (33,000 and 54,000 daltons), have been determined over the pH range 5.2-7.8, and found to be indistinguishable.
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U2 - 10.1016/0003-2697(80)90262-6
DO - 10.1016/0003-2697(80)90262-6
M3 - Article
C2 - 6770709
AN - SCOPUS:0019153412
VL - 103
SP - 235
EP - 239
JO - Analytical Biochemistry
JF - Analytical Biochemistry
SN - 0003-2697
IS - 1
ER -