| 摘要 |
A beta-alanine N-methyltransferase was isolated from L. latifolium. The purified enzyme catalyzes the N-methylation of beta-ala betaine, has an isoelectric point of about 5.15 and an apparent molecular weight of about 43 kilodaltons. The purified enzyme was partially sequenced. The purified enzyme or portions thereof can be used to make antibodies that specifically bind the enzyme, and can be introduced into a cell to modulate the cell's N-methyltransferase activity level and ability to resist environmental stress.
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