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Separation and some characterizations of NADPH-enoyl CoA reductase(s) from Candida albicans
- Source :
- Chemical and Pharmaceutical Bulletin. 22:2685-2691
- Publication Year :
- 1974
- Publisher :
- Pharmaceutical Society of Japan, 1974.
-
Abstract
- Two fractions containing NADPH-enoyl CoA reductase activities were isolated from crude extracts of Candida albicans. One fraction (Type-I) having larger molecular weight utilizes 5-hydroxyundec-cis-2-enoyl CoA, oct-cis-2-enoyl CoA and oct-trans-2-enoyl CoA as substrates with Km values of 2.5×10-6M, 1.1×10-6M and 5.0×10-7M, respectively, while another fraction (Type-II) having smaller molecular weight utilizes these substrates with Km values of 3.0×10-6M, 5.3×10-5M and 1.0×10-5M, respectively. This indicates that there exist comparable differences between these two in their affinities especially for the latter two substrates. Some characterizations, such as, effects of pH and of heat treatment on the activities of these reductase preparations were also investigated.
- Subjects :
- Hot Temperature
biology
Chemistry
Stereochemistry
Enoyl coA reductase
Fraction (chemistry)
General Chemistry
General Medicine
Hydrogen-Ion Concentration
Reductase
biology.organism_classification
Affinities
Kinetics
Biochemistry
Candida albicans
Undecylenic Acids
Drug Discovery
Coenzyme A
Oxidoreductases
Subjects
Details
- ISSN :
- 13475223 and 00092363
- Volume :
- 22
- Database :
- OpenAIRE
- Journal :
- Chemical and Pharmaceutical Bulletin
- Accession number :
- edsair.doi.dedup.....1d52ac4b0c6bd7b7b9de7d43e6ca52ec