CDNA cloning of Batis maritima methyl chloride transferase and purification of the enzyme.

ABSTRACT: Methyl chloride transferase catalyzes the synthesis of methyl chloride from S-adenosine-L-methionine and chloride ion. This enzyme has been purified 2,700-fold to homogeneity from Batis maritima, a halophytic plant that grows abundantly in salt marshes. The purification of the enzyme was accomplished by a combination of ammonium sulfate fractionation, column chromatography on Sephadex G100 and adenosine-agarose, and TSK-250 size-exclusion HPLC. The purified enzyme exhibits a single band on SDS/PAGE with a molecular mass of approximately 22.5 kDa. The molecular mass of the purified enzyme was 22,474 Da as determined by matrix-associated laser desorption ionization mass spectrometry. The methylase can function in either a monomeric or oligomeric form. A 32-aa sequence of an internal fragment

SUBMITTER: Ni X 

PROVIDER: S-EPMC23635 | biostudies-literature | 1998 Oct

REPOSITORIES: biostudies-literature