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KMID : 0380219950280050451
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Journal of Biochemistry and Molecular Biology
1995 Volume.28 No. 5 p.451 ~ p.457
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Isolation and Characterization of Four Carboxypeptidases in Canavalia lineata Cotyledons
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Yang Jong-Moon
Rhew Tae-Hyong
Koh Suck-Chan
Kwon Young-Myung
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Abstract
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Four carboxypeptidases, CP1, CP2, CP3, and CP4 were isolated from the cotyledons of germinating seedlings of Canavalia lineata by sequential chromatography on the following four columns: 1) CM-cellulose, 2) Sephacryl 5-300, 3) Procion red dye, and 4) Sephacryl S-200. A number of properties of the enzymes, such as substrate specificity, molecular weight, optimum pH, thermal stability, have been determined. Enzyme activities were measured using the Cbz(carbobenzoxy)-dipeptides containing phenylalanine at the penultimate position. The Km values of four carboxypeptidases for Cbz-Phe-Ala were 0.50, 0.65, 1.30, and 1.35 mM, respectively. The inhibition studies indicated that the four carboxypeptidases were all serine type. Each of the carboxypeptidases with molecular weights of 145, 114, 105, and 104 kDa, respectively, had the optimum enzyme activity at pH 5.0~6.0. And they were sensitive to high temperature.
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KEYWORD
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Canavalia lineata, carboxypeptidases, procion red, substrate specificity
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