Purification, Kinetic Properties, and cDNA Cloning of Mammalian Betaine-Homocysteine Methyltransferase*

@article{Garrow1996PurificationKP,
  title={Purification, Kinetic Properties, and cDNA Cloning of Mammalian Betaine-Homocysteine Methyltransferase*},
  author={T. Garrow},
  journal={The Journal of Biological Chemistry},
  year={1996},
  volume={271},
  pages={22831 - 22838}
}
  • T. Garrow
  • Published 1996
  • Biology, Medicine
  • The Journal of Biological Chemistry
    • Porcine liver betaine-homocysteine methyltransferase (BHMT; EC) was purified to homogeneity, and the Michaelis constants for betaine, dimethylacetothetin, and L-homocysteine are 23, 155, and 32 μM, respectively. The maximum rate of catalysis is 47-fold greater using dimethylacetothetin as a methyl donor compared with betaine. Partial amino acid sequence of porcine BHMT was obtained, and inosine-containing redundant oligonucleotide primers were used to amplify an 815-base pair sequence of the… CONTINUE READING
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    Highly Influential Citations
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    Background Citations
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    211 Citations
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