PURIFICATION AND CHARACTERIZATION OF FERREDOXIN FROM HYDROGENOBACTER-THERMOPHILUS STRAIN TK-6

Authors
ISHII M UEDA Y YOON KS IGARASHI Y KODAMA T
Citation
M. Ishii et al., PURIFICATION AND CHARACTERIZATION OF FERREDOXIN FROM HYDROGENOBACTER-THERMOPHILUS STRAIN TK-6, Bioscience, biotechnology, and biochemistry, 60(9), 1996, pp. 1513-1515
Citations number
15
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
Journal title
Bioscience, biotechnology, and biochemistry → ACNP
ISSN journal
09168451
Volume
60
Issue
9
Year of publication
1996
Pages
1513 - 1515
Database
ISI
SICI code
0916-8451(1996)60:9<1513:PACOFF>2.0.ZU;2-M
Abstract
Ferredoxin was purified from cells of Hydrogenobacter thermophilus str ain TK-6. Purification was performed aerobically by the addition of oc tyl-beta-glucoside to the buffers, The purified ferredoxin had a molec ular mass of 13,000 and contained a [4Fe-4S] cluster. The protein had a long stretch at the N-terminal region; however, the sequence was not similar to the sequences of ferredoxins with a long stretch from Arch aebacteria.