PURIFICATION AND PROPERTIES OF INTACT HYDROGENASE FROM DESULFOVIBRIO-VULGARIS (MIYAZAKI)

Authors
KAMACHI T UNO S HIRAISHI T OKURA I
Citation
T. Kamachi et al., PURIFICATION AND PROPERTIES OF INTACT HYDROGENASE FROM DESULFOVIBRIO-VULGARIS (MIYAZAKI), Journal of molecular catalysis. A, Chemical, 95(1), 1995, pp. 93-98
Citations number
13
Categorie Soggetti
Chemistry Physical
Journal title
Journal of molecular catalysis. A, Chemical → ACNP
ISSN journal
13811169
Volume
95
Issue
1
Year of publication
1995
Pages
93 - 98
Database
ISI
SICI code
1381-1169(1995)95:1<93:PAPOIH>2.0.ZU;2-6
Abstract
The intact hydrogenase from Desulfovibrio vulgaris (Miyazaki) was puri fied and characterized. The purified hydrogenase had a molecular weigh t of 92.0 kDa, with two different subunits (Mw = 62.5 kDa and 29.5 kDa ). The molecular weight of the large subunit of the intact hydrogenase was 2 kDa larger than the tryptic digested hydrogenase. The absorptio n spectrum and the EPR spectrum of the intact hydrogenase were identic al to those of tryptic digested hydrogenase. Phase separation study in dicated the detergent solubilized hydrogenase was more hydrophobic tha n tryptic digested hydrogenase.