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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.
Subject(s)
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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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