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嚴翼都,金福亮,白汶基 圓光大學校 醫科學硏究所 1986 圓光醫科學 Vol.2 No.2
The enzymatic carboxyl methyl esterification of red blood cell (RBC) membrane protein has been investigated in the isolated membrane and intact rat RBC population of different ages separated by density gradient centrifugation. The activity of cytosolic protein methylase Ⅱ was decreased according to the cell ageing, but isolated membrane protein from RBC of different age showed an age-related increased ability to act as methyl accepting substrates. Membrane proteins were shown to be the natural and excellent substrates for the cytosolic protein methylase Ⅱ compared with protein methylase Ⅰ and Ⅲ in the RBC cell so that the carboxyl methylation of membrane protein was the major methylating reactions in vitro and vivo. When RBC were incubated with media containing L-[methyl-^3H] methionine and 16.7 mM glucose, the [^3H]-methyl incorporation into the carboxyl group of membrane protein was 3.12 pmole/㎎ protein but incubated with media containing L-[methyl -^3H] methionine and 5.6 mM glucose, the amount of carboxyl methylation was 2.36 prnole/㎎ protein. About 1.4 fold increase in membrane protein carboxyl methylation was observed in intact younger RBC in comparison with intact older RBC in above media.