NAD-DEPENDENT GLUTAMATE-DEHYDROGENASE FROM THE THERMOPHILIC EUBACTERIUM BACILLUS-ACIDOCALDARIUS

被引：4

作者：

CONSALVI, V

CHIARALUCE, R

MILLEVOI, S

PASQUO, A

POLITI, L

DEROSA, M

SCANDURRA, R

机构：

[1] UNIV ROMA LA SAPIENZA, DIPARTIMENTO SCI BIOCHIM A ROSSI FANELLI, I-00185 ROME, ITALY

[2] UNIV LAQUILA, DIPARTIMENTO SCI & TECHNOL BIOMED & BIOMETRIA, LAQUILA, ITALY

[3] UNIV NAPLES, FAC MED & CHIRURG 1, IST BIOCHIM MACROMOLEC, NAPLES, ITALY

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1994年 / 109卷 / 04期

关键词：

BACILLUS ACIDOCALDARIUS; GLUTAMATE DEHYDROGENASE; NAD-DEPENDENT DEHYDROGENASE; PROTEIN PURIFICATION; THERMOPHILIC ENZYME; THERMOPHILIC EUBACTERIUM;

D O I：

10.1016/0305-0491(94)90132-5

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：

The first thermophilic eubacterial glutamate dehydrogenase was purified to homogeneity from Bacillus acidocaldarius to compare its molecular properties with those of the glutamate dehydrogenase from thermophilic archaea. Glutamate dehydrogenase represents 2% of the total soluble proteins of B. acidocaldarius, an amount that may suggest an important role for this enzyme in nitrogen metabolism of the thermophilic eubacterium. The protein is a hexamer (subunit mass 48 kDa) and undergoes dissociation during gel filtration analysis. Isoelectric focusing of the purified enzyme indicated a pI of 4.5. The enzyme is strictly specific for NAD, 2-oxoglutarate, and L-glutamate. The thermal stability of B. acidocaldarius glutamate dehydrogenase is dependent on protein concentration.

引用

页码：691 / 699

页数：9

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