Localization and Turnover Studies of Membrane Nicotinamide Adenine Dinucleotide Glycohydrolase in Rat Liver

作者: K.W. Bock , P. Siekevitz , G.E. Palade

DOI: 10.1016/S0021-9258(18)62548-7

关键词: Gel electrophoresisHepatocyteBiologyNicotinamide adenine dinucleotideCytochrome b5SephadexBiochemistryMicrosomeCell fractionationMolecular biologyEndoplasmic reticulum

摘要: Abstract Cell fractionation experiments indicate that NAD glycohydrolase (EC 3.2.2.6) is a constituent enzyme of both the microsomal (endoplasmic reticulum) and plasmalemma membrane rat hepatocyte. The was solubilized by steapsin digestion from fractions subsequently purified ∼2000 over homogenate ∼500 fraction successive DEAE-cellulose, Sephadex G-100 chromatography, polyacylamide gel electrophoresis. heterogeneous mixture proteins with two or three major components. apparent half-life determined to be ∼18 days use double labeling procedure uniformly labeled 14C-l-leucine 3H-(4,5)-l-leucine. results add another protein list those (NADPH-cytochrome c reductase, cytochrome b5) known turn asynchronously in endoplasmic reticulum membrane. No gross differences were found between plasmalemmal glycohydrolase.

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