Identification of a non-microsomal cinnamic acid 4-hydroxylase from potato tuber (S. tuberosum) and its partial purification.
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.
Deshpande
A S
AS
Food Technology and Enzyme Engineering Division, Bhabha Atomic Research Centre, Bombay.
Surendranathan
K K
KK
Nair
P M
PM
D002413:Cations, Divalent; D002458:Cell Fractionation; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D011198:Solanum tuberosum / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D050564:Trans-Cinnamate 4-Monooxygenase
D002413:Cations, Divalent; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D050564:Trans-Cinnamate 4-Monooxygenase