PURIFICATION AND PROPERTIES OF EXTREMELY THERMOSTABLE GLUTAMATE-DEHYDROGENASES FROM 2 HYPERTHERMOPHILIC ARCHAEBACTERIA, PYROCOCCUS-WOESEI AND PYROCOCCUS-FURIOSUS

被引：44

作者：

OHSHIMA, T

NISHIDA, N

机构：

[1] Department of Chemistry, Kyoto University of Education, Kyoto 612, Fukakusa, Fushimi-ku

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1993年 / 57卷 / 06期

关键词：

D O I：

10.1271/bbb.57.945

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：

Glutamate dehydrogenase (L-glutamate: NADP oxidoreductase, deaminating, EC 1.4.1.4) from the hyperthermophilic archaebacteria Pyrococcus woesei and P. furiosus were purified to homogeneity from crude extracts. The enzymes had similar enzymological properties: molecular mass, subunit structure, optimum pHs for the oxidative deamination and reductive amination, substrate specificity and coenzyme specificity as well as thermostability; the activity was not lost after incubation at 105-degrees-C for 30 min. However, some differences were detected in resistance to urea denaturation and effects of salts on their activity and stability. The N-terminal 20 amino acid sequences of the two enzymes were identical.

引用

页码：945 / 951

页数：7

共 20 条

[1] CULTIVATION TECHNIQUES FOR HYPERTHERMOPHILIC ARCHAEBACTERIA - CONTINUOUS CULTURE OF PYROCOCCUS-FURIOSUS AT TEMPERATURES NEAR 100-DEGREES-C [J].