TY - JOUR
T1 - Purification and characterization of benzoyl-l-arginine p-nitroanilide hydrolase from etiolated leaves of Zea mays
AU - Doi, Michio
AU - Shioi, Yuzo
AU - Sasa, Tsutomu
PY - 1986/11/1
Y1 - 1986/11/1
N2 - Benzoyl-l-arginine p-nitroanilide hydrolase in the etiolated leaves of Zea mays L. has been purified 1,266-fold by a combination of gel filtration, ion exchange, and hydrophobic chromatography with a recovery of 13%. The specific activity of the purified enzyme is 5.7 units/mg protein. The enzyme is an acidic protein with a pI value of 4.6 and optimum pH of 8.2. The molecular weight of the enzyme was estimated to be 59,000. Substrate inhibition was observed at a concentration higher than 30 μM BAPA and the apparent Km for BAPA was 29 μM at pH 8.0. The enzyme activity was inhibited by sulfhydryl reagents, leupeptin, antipain, and N-tosyl-l-lysine chloromethyl ketone. The inhibitor study suggests that the enzyme belongs to the class of the sulfhydryl proteases.
AB - Benzoyl-l-arginine p-nitroanilide hydrolase in the etiolated leaves of Zea mays L. has been purified 1,266-fold by a combination of gel filtration, ion exchange, and hydrophobic chromatography with a recovery of 13%. The specific activity of the purified enzyme is 5.7 units/mg protein. The enzyme is an acidic protein with a pI value of 4.6 and optimum pH of 8.2. The molecular weight of the enzyme was estimated to be 59,000. Substrate inhibition was observed at a concentration higher than 30 μM BAPA and the apparent Km for BAPA was 29 μM at pH 8.0. The enzyme activity was inhibited by sulfhydryl reagents, leupeptin, antipain, and N-tosyl-l-lysine chloromethyl ketone. The inhibitor study suggests that the enzyme belongs to the class of the sulfhydryl proteases.
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U2 - 10.1016/0003-9861(86)90737-X
DO - 10.1016/0003-9861(86)90737-X
M3 - Article
C2 - 3535677
AN - SCOPUS:0022808964
VL - 250
SP - 358
EP - 363
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -