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Hematin as an Inhibitor of Erythroid Cell Mambrane - Bound Enzymes
김성식,박시원,이민화,조용호 생화학분자생물학회 1973 BMB Reports Vol.3 No.2
Previous studies from this laboratory demonstrated that hematin is a potent inhibitor of NAD nucieosidase in the membrane fraction of rabbit erythrocytes. In the present studies, it was found that hematin also inhibited markedly the membranebound adenosine triphosphatase of erythrocytes and the inhibitor-free ribonuclease present in the membrane fraction of rabbit reticulocytes. In contrast to the membrane-bound enzymes, ADP-ribose pyrophosphatase, a soluble enzyme in rabbit erythrocytes, was not inhibited by hematin. Similarly, crude soluble ribonuclease in reticulocytes was not so markedly inhibited by hematin as the membrane-bound ribonuclease. Hematin was also found to be a potent hemolytic agent, the concentration for hemolysis being much less than that required for NADase inhibition. The hemolytic effect of sodium deoxycholate was roughly correlated with their inhibitory effectiveness on NADase. These results suggest that hematin is an universal, rather than any specific, inhibitor of the membrane-bound enzymes. It appears likely that the inhibitory effect of hematin on the membrane-bound erythroid cell enzymes is due to changes in membrane structure itself brought about by hematin.