Liver plasma membrane enzyme activities following glutaraldehyde fixation

Pathology ◽  
1976 ◽  
Vol 8 (1) ◽  
pp. 43-45 ◽  
Author(s):  
P.J. Hertzog ◽  
R.N. Le Page ◽  
P.S. Bhathal
Keyword(s):  
Plasma Membrane ◽  
Enzyme Activities ◽  
Glutaraldehyde Fixation ◽  
Liver Plasma Membrane ◽  
Membrane Enzyme

Effect of vanadate on rat myometrium plasma membrane enzyme activities

1980 ◽  
Vol 58 (10) ◽  
pp. 1247-1250 ◽  
Author(s):  
A. K. Grover ◽  
T. R. Jones ◽  
E. E. Daniel
Keyword(s):  
Plasma Membrane ◽  
Enzyme Activities ◽  
Contractile Activity ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Membrane Enzyme ◽  
Ca Uptake ◽  
Vanadate Inhibition ◽  
Inhibited Acid ◽  
Isolated Rat

Vanadate inhibited K+-activated and K+-activated ouabain-sensitive p-nitrophenyl phosphatases of rat myometrium at nanomolar concentrations. The vanadate concentrations required for 50% inhibition were 220 ± 30 nM for the K+-activated component of this enzyme and 200 ± 30 nM for the K+-activated ouabain-sensitive component. Micromolar concentrations of vanadate inhibited acid and alkaline p-nitrophenyl phosphatases. ATP-dependent Ca uptake by the plasma membrane vesicles was not inhibited by 10 nM – 1 mM vanadate. Mg2+-ATPase was also not affected. Thus K+-activated and K+-activated ouabain-sensitive p-nitrophenyl phosphatase activities of the plasma membrane were most sensitive to inhibition by vanadate. Preliminary experiments demonstrated that similar to ouabain, vanadate inhibited potassium-induced abolition of spontaneous contractile activity of isolated rat myometrium in K-free Krebs. This effect of vanadate is consistent with vanadate inhibition of K+-activated ouabain-sensitive p-nitrophenyl phosphatase.

Modulation of Morphology and Plasma-Membrane Enzyme Activities of Rat Thymocytes Induced by Specific Antisera

Immunobiology ◽  
1982 ◽  
Vol 160 (5) ◽  
pp. 403-412
Author(s):  
H.C. Bauer ◽  
V. Speth ◽  
E. Ferber ◽  
U. Hurtenbach
Keyword(s):  
Plasma Membrane ◽  
Enzyme Activities ◽  
Membrane Enzyme ◽  
Specific Antisera
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