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백문기,Deibler, G.E.,Martenson, R.E.,Kies, M.W. 충남대학교 의과대학 지역사회의학연구소 1980 충남의대잡지 Vol.7 No.2
S-adenosyl-L-methionine : protein arginine N-methyltransferase having an optimum pH around 7.2 has been purified approximately 1,800 fold with 16% yield from wheat germ, and an attempt was made to resolve controversial multiplicity on the enzyme. The end products of the purified enzyme preparation were N^G-monomethylarginine and N^G, N'^G-dimethylarginine in a ratio of 70 : 30, and the enzyme preparation lost the ability of less purified ones to carry out the synthesis of N^G, N^G-dimethylarginine, strongly indicating that different enzymes were responsible for the production of different methylated derivatives of arginine. Contrary to our expectation, histone was better substrate than myelin basic proteins from various sources. From the above results and products ratio change at each step of purification, we discussed the possibility that three enzymes were involved in the formation of three methylated arginine derivatives which has been identified so far.
Paik, Moon Kee,Deibler. Glady,Martenson, Russel E.,Kies, Marian W 생화학분자생물학회 1986 BMB Reports Vol.13 No.4
S-adenosyl-L-methionine : protein arginine N-methyltransferase (EC 2. 1. 1. 23) having an optimum pH around 7, 2 has been purified approximarely 1,800-fold with a 16% yield, The purified enzyme preparation is completely free of any other protein methyltransferases. The end products of crude enzyme preparation after hydrolysis are N^G-monomethyl, N^G, N^G-dimethyl, and N^G, N^G-dimethylarginine, but the purified enzyme preparation lose the ability of less purified one to carry out the synthesis of N^G, N^G-dimethylarginine, indicating that the enzyme responsible for N^G, N^G-dimethylarginine is disappeared and therefore more than a single enzyme is involved in the synthesis of the methylated arginine derivatives, The relative substrate efficiency of myelin basic protein of various sourcess appears to be less active than that of histories, as well as less N^G, N^G-dimethylarginine is formed in myelin basic protein than in histories, From the above results and uneven distribution of the methylated arginine derivatives, we discuss the possibility that the methylated arginine derivatives are for formed by three different methylases.