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KMID : 0371619860020020161
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Journal of Wonkwang Medical Science
1986 Volume.2 No. 2 p.161 ~ p.172
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Carboxyl Methylation of Membrane Protein in Rat Red Blood Cells
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Abstract
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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 trom 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-Cmethyl-´H) methionine and 16.7 mM glucose, the (3H)-methyl incorporation into the carboxyl group of membrane protein was, 3.12 pmole /fng protein but incubated with media containing L-Cmethyl-3H) methionine and 5.6 mM glucose, the amount of carboxyl r,lethylation was 2.86 pmole/mg 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.
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