TY - JOUR
T1 - N-acetyl-(L-Ala)3-p-nitroanilide as a new chromogenic substrate for elastase
AU - Feinstein, Gad
AU - Kupfer, Abraham
AU - Sokolovsky, Mordechai
PY - 1973/2/20
Y1 - 1973/2/20
N2 - The introduction of a useful new chromogenic substrate for the determination of elastase (EC 3.4.4.7) activity is described. N-acetyl-L-Ala-L-Ala-L-Ala-p-nitroanilide (AcAla3NA) is a new specific elastase substrate whose hydrolysis can be followed spectrophotometrically at 410 nm in a wide pH range. Its rate of hydrolysis by α-chymotrypsin (EC 3.4.4.5) and trypsin (EC 3.4.4.4.) is 0.02% and 0.001% respectively compared to its rate of hydrolysis by elastase. As little as 0.1 μg elastase/ml can be satisfactorily determined. At pH 8, Km = 0.88 mM and kcat = 11.9 sec-1.
AB - The introduction of a useful new chromogenic substrate for the determination of elastase (EC 3.4.4.7) activity is described. N-acetyl-L-Ala-L-Ala-L-Ala-p-nitroanilide (AcAla3NA) is a new specific elastase substrate whose hydrolysis can be followed spectrophotometrically at 410 nm in a wide pH range. Its rate of hydrolysis by α-chymotrypsin (EC 3.4.4.5) and trypsin (EC 3.4.4.4.) is 0.02% and 0.001% respectively compared to its rate of hydrolysis by elastase. As little as 0.1 μg elastase/ml can be satisfactorily determined. At pH 8, Km = 0.88 mM and kcat = 11.9 sec-1.
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U2 - 10.1016/0006-291X(73)91508-8
DO - 10.1016/0006-291X(73)91508-8
M3 - Article
C2 - 4734817
AN - SCOPUS:0015930533
SN - 0006-291X
VL - 50
SP - 1020
EP - 1026
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -