NICOTINAMIDE ADENINE-DINUCLEOTIDE SPLITTING ENZYME - PLASMA-MEMBRANE PROTEIN OF MURINE MACROPHAGES
NICOTINAMIDE ADENINE-DINUCLEOTIDE SPLITTING ENZYME - PLASMA-MEMBRANE PROTEIN OF MURINE MACROPHAGES
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DOI：
10.1016/0003-9861(79)90333-3
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发表时间：
1979-01-01
影响因子：
3.9
通讯作者：
SEELEY, RJ
中科院分区：
文献类型：
--
作者：
ARTMAN, M;SEELEY, RJ
The subcellular distribution of NADase in splenic and peritoneal macrophages of the mouse was studied. Conventional procedures for fractionation and isolation of subcellular components demonstrated that the NADase of murine macrophages was localized in the microsomal fraction. Using the diazonium salt of sulfanilic acid, a nonpenetrating reagent known to inactivate ecto-enzymes in intact cells, purified plasma membrane preparations and marker enzymes, 5''-nucleotidase for plasma membrane and glucose 6-phosphatase for the microsomal fraction, it was shown that NADase of murine macrophages is a plasma membrane ecto-enzyme and the microsomal fraction is a mixture of endoplasmic reticulum and plasma membrane elements. At 5 .times. 10-4 M concentration, the diazonium salt of sulfanilic acid drastically decreased NADase in intact splenic and peritoneal macrophages of the mouse. 5''-Nucleotidase was similarly inhibited by this reagent; the activity of glucose 6-phosphatase remained unaffected. There was a good recovery of NADase of high specific activity in plasma membrane preparations that were characterized by high 5''-nucleotidase and low glucose 6-phosphatase activity.
