BMB Reports
- Volume 30 Issue 6
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- Pages.410-414
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- 1997
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- 1976-670X(eISSN)
Purification and Characterization of Protein Carboxyl O-Methyltransferase from Porcine Spleen
- Yoon, Sung-Pil (Department of Genetic Engineering, College of Life Sdence and Natural Resources) ;
- Son, Min-Sik (Department of Genetic Engineering, College of Life Sdence and Natural Resources) ;
-
Han, Jeung-Whan
(Laboratory of Biochemistry, College of Pharmacy, Sung Kyun Kwan University)
;
- Lee, Hyang-Woo (Laboratory of Biochemistry, College of Pharmacy, Sung Kyun Kwan University) ;
- Hong, Sung-Youl (Department of Genetic Engineering, College of Life Science and Natural Resources)
- Received : 1997.01.08
- Published : 1997.11.30
Abstract
We purified a protein carboxyl O-methyltransferase (protein methylase II) from porcine spleen to homogeneity. The molecular weight of the porcine spleen protein methylase II (ps-PM II) was estimated to be 27,500 daltons on SDS-PAGE. Amino acid sequence of N-terminal 28 residues for ps-PM II was identified. Amino-terminal three amino acid residues of ps-PM II were deleted when compared to those of other protein carboxyl methytransferase. S-Adenosyl-L-homocysteine competitively inhibits ps-PM II with a K, value of