scholarly journals Pentitol metabolism of Rhodobacter sphaeroides Si4: purification and characterization of a ribitol dehydrogenase

1992 ◽  
Vol 138 (6) ◽  
pp. 1277-1281 ◽  
Author(s):  
C. Kahle ◽  
K.-H. Schneider ◽  
F. Giffhorn
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Purification And Characterization ◽  
Ribitol Dehydrogenase

Purification and characterization of Rhodobacter sphaeroides acyl carrier protein

Biochemistry ◽  
1987 ◽  
Vol 26 (10) ◽  
pp. 2740-2746 ◽  
Author(s):  
Cynthia L. Cooper ◽  
Stephen G. Boyce ◽  
Donald R. Lueking
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Purification And Characterization

scholarly journals Purification and Characterization of the Flagellar Basal Body of Rhodobacter sphaeroides

2003 ◽  
Vol 185 (17) ◽  
pp. 5295-5300 ◽  
Author(s):  
K. Kobayashi ◽  
T. Saitoh ◽  
D. S. H. Shah ◽  
K. Ohnishi ◽  
I. G. Goodfellow ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Basal Body ◽  
Protein Identification ◽  
Gene Clusters ◽  
Growth Conditions ◽  
Heterotrophic Growth ◽  
Purification And Characterization ◽  
Heat Stable ◽  
Acid Labile

ABSTRACT Flagellar hook-basal body (HBB) complexes were purified from Rhodobacter sphaeroides. The HBB was more acid labile but more heat stable than that of Salmonella species, and protein identification revealed that HBB components were expressed only from one of the two sets of flagellar gene clusters on the R. sphaeroides genome, under the heterotrophic growth conditions tested here.

Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase fromRhodobacter sphaeroidesOU5

2008 ◽  
Vol 54 (10) ◽  
pp. 829-834 ◽  
Author(s):  
N. K. Ranjith ◽  
Ch. V. Ramana ◽  
Ch. Sasikala
Keyword(s):  
Molecular Mass ◽  
Rhodobacter Sphaeroides ◽  
Purification And Characterization ◽  
Low Concentrations ◽  
Sds Page ◽  
Dopa Formation

An enzyme involved in the catabolism of 3,4-dihydroxyphenylalanine (DOPA) was isolated from Rhodobacter sphaeroides OU5. The enzyme catalyzes the formation of 3,4-dihydroxyphenylpyruvic acid (DOPP) and ammonia from DOPA. Formation of ammonia by DOPA oxidative deaminase was O2dependent and the enzyme isolated to its homogeneity has 100% affinity for DOPA. DOPA oxidative deaminase is functional at low concentrations of the substrate (<100 μmol·L–1) and is independent of NADH. The molecular mass of the purified enzyme is ~190 kDa and the enzyme could be a pentamer of 54, 42, 34, 25, and 23 kDa subunits as determined by SDS–PAGE.

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