ISSN:
1573-6881
Keywords:
Cytochrome oxidase
;
Azotobacter vinelandii
;
phospholipid activation
;
cytochromec 4:o oxidase
;
phosphatidylethanolamine
;
TMPD oxidase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract A modified procedure is described that was used to solubilize and purify the TMPD-dependent cytochromec 4:o oxidase fromAzotobacter vinelandii. Two functional components (Fractions I and V) were obtained after DEAE-cellulose chromatography. Fraction V contained both cytochromec 4 (3.6 nmol/mg protein) and cytochromeo (1.6 nmol/mg protein). This cytochrome oxidase complex oxidized TMPD at “moderate” rates. Fraction I, a clear greenish-yellow fraction, contained primarily phosphatidylethanolamine with some phosphatidylglycerol. Fraction I itself could not oxidize TMPD, but when it was preincubated with Fraction V, a 2–4-fold stimulation in TMPD oxidase activity occurred. Other “authentic” micellar phospholipids also readily activited TMPD oxidase activity in Fraction V. Themaximum activation effect obtained with Fraction I was in essence duplicated with purified phosphatidylethanolamine.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00743240
Permalink
