Identification of a non-microsomal cinnamic acid 4-hydroxylase from potato tuber (S. tuberosum) and its partial purification.
Indian J Biochem Biophys
;
1992 Oct; 29(5): 418-24
Article
in English
| IMSEAR
| ID: sea-27787
ABSTRACT
The cytoplasmic localisation of cinnamic acid 4-hydroxylase (CA4H) has been shown by isolation and subcellular fractionation of the enzyme in Hepes buffer. The enzyme was purified by ammonium sulphate fractionation followed by AcA-34 molecular sieve chromatography. The enzyme existed as a high molecular mass which dissociated to a lower form on dilution on the column. The pH optimum, sulphydryl requirement, molecular and preliminary kinetic characteristics were investigated.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Subcellular Fractions
/
Solanum tuberosum
/
Kinetics
/
Cations, Divalent
/
Cell Fractionation
/
Cytochrome P-450 Enzyme System
/
Trans-Cinnamate 4-Monooxygenase
/
Hydrogen-Ion Concentration
/
Mixed Function Oxygenases
/
Microsomes
Type of study:
Prognostic study
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1992
Type:
Article
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