Abstract
gamma-Tocopherol methyltransferase was solubilized and purified from Capsicum chromoplast membranes by a combination of standard fractionation techniques. The purified enzyme was electrophoretically homogeneous, and its molecular weight, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was 33,000. In the absence of detergent, the enzyme formed high molecular weight aggregates. Several properties of the enzyme have been determined. The Km values were 2.5 and 13.7 microM for S-adenosylmethionine and gamma-tocopherol, respectively. The enzyme was able to transfer the methyl group S-adenosylmethionine to N-4-azido-2-nitrophenyl-beta-alanyl-gamma-tocopherol. The rate of transfer was less efficient compared to gamma-tocopherol. In the presence of ultraviolet light, this analog inhibited the gamma-tocopherol methyltransferase activity.
Highlights
Its molecular weight, determined by sodium dode- Effect of pH-The effect of pH on the activity of y-tocy1 sulfate-polyacrylamide gel electrophoresis, was copherol methyltransferase was evaluated in the pHrange of
We solubilized the y-tocopherol methyltransferase from Capsicum chromoplasts with no loss enzymatic since the boiled preparation failed to perform this conversion. These data indicate that the modification of the hydroxy group of y-tocopherol is not strictly deleterious to the methylation reaction
We describe here the purification to homogeneity and some molecular and catalytic properties of the ytocopherol methyltransferase from Capsicum chromoplasts
Summary
PURIFICATION AND CHARACTERIZATION OF ./-TOCOPHEROL METHYLTRANSFERASE FROM CAPSICUM CHROMOPLASTS*. We solubilized the y-tocopherol methyltransferase from Capsicum chromoplasts with no loss enzymatic since the boiled preparation failed to perform this conversion. These data indicate that the modification of the hydroxy group of y-tocopherol is not strictly deleterious to the methylation reaction. Point and on the biogenoefsiys-tocopherol methyltransferase in plantcells are underway
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