NADP efficiently inhibits endogenous but not pertussis toxin-catalyzed covalent modification of membrane proteins incubated with NAD.
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NADP efficiently inhibits endogenous but not pertussis toxin-catalyzed covalent modification of membrane proteins incubated with NAD. / Rosenthal, W; Binder, Thomas; Schultz, G.
in: FEBS LETT, Jahrgang 211, Nr. 2, 2, 1987, S. 137-143.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - NADP efficiently inhibits endogenous but not pertussis toxin-catalyzed covalent modification of membrane proteins incubated with NAD.
AU - Rosenthal, W
AU - Binder, Thomas
AU - Schultz, G
PY - 1987
Y1 - 1987
N2 - Incubation of membranes of human erythrocytes and platelets but not of human neutrophils with [32P]NAD leads to covalent modification of various membrane proteins and of added albumin. In membranes of all three cell types, pertussis toxin (PT), in the presence of NAD, specifically labelled a 40 kDa peptide, i.e. the alpha-subunit of a guanine nucleotide-binding protein. This effect of PT was slightly reduced by NADP, whereas modification of other membrane proteins and of albumin was largely suppressed, independent of whether PT was present or not. Labelling of cytosolic proteins in the presence of NAD was marginal; only in neutrophil cytosol, PT modified a 40 kDa peptide. Membranes of erythrocytes and platelets exhibited NAD-degrading activity, which was inhibited by NADP. The data suggest a high substrate specificity of PT for NAD. Inhibition of endogenous enzymes by NADP may prove useful for the evaluation of PT substrates.
AB - Incubation of membranes of human erythrocytes and platelets but not of human neutrophils with [32P]NAD leads to covalent modification of various membrane proteins and of added albumin. In membranes of all three cell types, pertussis toxin (PT), in the presence of NAD, specifically labelled a 40 kDa peptide, i.e. the alpha-subunit of a guanine nucleotide-binding protein. This effect of PT was slightly reduced by NADP, whereas modification of other membrane proteins and of albumin was largely suppressed, independent of whether PT was present or not. Labelling of cytosolic proteins in the presence of NAD was marginal; only in neutrophil cytosol, PT modified a 40 kDa peptide. Membranes of erythrocytes and platelets exhibited NAD-degrading activity, which was inhibited by NADP. The data suggest a high substrate specificity of PT for NAD. Inhibition of endogenous enzymes by NADP may prove useful for the evaluation of PT substrates.
M3 - SCORING: Zeitschriftenaufsatz
VL - 211
SP - 137
EP - 143
JO - FEBS LETT
JF - FEBS LETT
SN - 0014-5793
IS - 2
M1 - 2
ER -
