PURIFICATION AND CHARACTERIZATION OF RAT-LIVER TRANSGLUTAMINASE

被引：20

作者：

WONG, WSD ^{[1
]}

BATT, C ^{[1
]}

KINSELLA, JE ^{[1
]}

机构：

[1] CORNELL UNIV,INST FOOD SCI,ITHACA,NY 14853

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1990年 / 22卷 / 01期

关键词：

D O I：

10.1016/0020-711X(90)90077-G

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. 1. Transglutaminase (EC 2.3.2.13) was purified from rat liver. 2. 2. The enzyme was stable at 25°C in the pH range of 6.0-9.0, with the optimum at pH9.0. 3. 3. The enzyme was inactivated after incubation for 20,4 and 1 min at 44°C, 52°C, and 60°C, respectively. 4. 4. Activation energies were 30.4 kcal/mol for denaturation and 19.9 kcal/mol for substrate conversion to products. 5. 5. The enzyme was inactivated by sulfhydryl modification with hydroxymercuribenzoate (99.1%) and N-ethymalemide (78.5%). 6. 6. Calcium, required for the activity, was replaced to a lesser extent, by Mg2+, Sr2+, Zn2+ and Mn2+ (31.8, 27.0, 24.6 and 3.5%). 7. 7. Steady-state kinetics showed: Vmax = 10 μM-min-1, Km = 0.05mM (N-dimethylated casein), kcat = 31.9min-1 and kcat km = 560 min-1mM-1. © 1990.

引用

页码：53 / 59

页数：7

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[2]

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