Dependence of pyridine nucleotide transhydrogenase on phospholipids and its sensitivity to N-ethylmaleimide |
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Authors: | Raymond L. Houghton Robert J. Fisher D. Rao Sanadi |
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Affiliation: | 1. Department of Cell Physiology, Boston Biomedical Research Institute 20 Staniford Street, Boston, Massachusetts 02114 USA;2. Department of Biological Chemistry, Harvard Medical School USA |
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Abstract: | A partially purified preparation of pyridine nucleotide transhydrogenase (E.C. 1.6.1.1.) (energy-independent) has been obtained from membranes of by means of deoxycholate extraction and DEAE-cellulose chromatography in the presence of Triton X-100. The enzyme was lipid-depleted by treating with cholate and ammonium sulfate. The preparation was reactivated by various phospholipids, in particular, bacterial cardiolipin and phosphatidyl glycerol. Phosphatidyl ethanolamine, the major phospholipid in the outer membrane of , was relatively ineffective in stimulating activity. The membrane-bound pyridine nucleotide transhydrogenase is slowly inhibited by N-ethylmaleimide. Protection against inhibition was achieved with NAD+ and NADP+, but NADPH served to accelerate the rate of inhibition. |
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Keywords: | relaxed strain stringent (wild type) strain SMG serine + methionine + glycine |
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