Myelin basic protein inhibits histone-specific protein methylase I
- Authors
- Park G.-H.; Chanderkar L.P.; Paik W.K.; Kim S.
- Issue Date
- 1986
- Keywords
- (Brain); Enzyme inhibitor; Histone-specific protein methylase I; Myelin basic protein; Protein-arginine-methyltransferase
- Citation
- Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, v.874, no.1, pp 30 - 36
- Pages
- 7
- Indexed
- SCOPUS
- Journal Title
- Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
- Volume
- 874
- Number
- 1
- Start Page
- 30
- End Page
- 36
- URI
- https://scholarworks.korea.ac.kr/kumedicine/handle/2020.sw.kumedicine/27642
- DOI
- 10.1016/0167-4838(86)90098-1
- ISSN
- 0167-4838
- Abstract
- Bovine brain myelin basic protein, free of associated proteolytic activity, was found to be a specific inhibitor of histone-specific protein methylase I (S-adenosyl-l-methionine:protein-l-arginine N-methyltransferase, EC 2.1.1.23) purified from bovine brain. 50% of the methyl group incorporation into the histone substrate catalyzed by the methylase I was inhibited by myelin basic protein at a concentration of 0.326 mM. However, neither of the peptide fragments (residues 1-116 and residues 117-170) generated by the chemical cleavage of myelin basic protein at the tryptophan residue retained the inhibitory activity for histone-specific protein methylase I. Proteins such as γ-globulin, bovine serum albumin, bovine pancreatic ribonuclease and polyarginine did not exhibit significant inhibitory activity toward the enzyme. The Ki value for myelin basic protein was estimated to be 3.42 · 10-5 M for histone-specific protein methylase I and the nature of the inhibition was uncompetitive toward histone substrate. © 1986.
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Collections - 1. Basic Science > Department of Biochemistry and Molecular Biology > 1. Journal Articles
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