THE N-TERMINAL AMINO-ACID-SEQUENCES OF BREVIBACTERIUM SP R312 NITRILE HYDRATASE

被引：10

作者：

DURAN, R ^{[1
]}

CHION, CKNCK ^{[1
]}

BIGEY, F ^{[1
]}

ARNAUD, A ^{[1
]}

GALZY, P ^{[1
]}

机构：

[1] ECOLE NATL SUPER AGRON MONTPELLIER,CHAIRE MICROBIOL IND & GENET MICROORGANISMES,PL VIALA,F-34060 MONTPELLIER 1,FRANCE

来源：

JOURNAL OF BASIC MICROBIOLOGY | 1992年 / 32卷 / 01期

关键词：

D O I：

10.1002/jobm.3620320104

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Nitrile hydratase from Brevibacterium sp. R312 was purified to homogeneity. The isoelectric point was 5.75. The two kinds of subunits were separated by reverse phase HPLC and their N-terminal amino acid sequences were found to be identical to those of Rhodococcus sp. N-774 nitrile hydratase.

引用

页码：13 / 19

页数：7

共 18 条

[1]

ANDREWS AT, 1986, ELECTROPHORESIS THEO, P26

[2]

ARNAUD A, 1976, CR ACAD SCI D NAT, V283, P571

[3] MICROBIAL DEGREDATION OF NITRILE COMPOUNDS .5. ALIPHATIC NITRILE HYDRATASE FROM ARTHROBACTER SP J-1 PURIFICATION AND CHARACTERIZATION [J].