Chapter 6 Oxidase control of plasma membrane proton transport

1996 ◽  
pp. 169-186 ◽  
Author(s):  
Frederick L. Crane ◽  
Iris L. Sun ◽  
Ruth A. Crowe ◽  
Hans Löw
Keyword(s):  
Plasma Membrane ◽  
Proton Transport

scholarly journals Effects of Abnormal-Sterol Accumulation onUstilago maydis Plasma Membrane H+-ATPase Stoichiometry and Polypeptide Pattern

1998 ◽  
Vol 180 (2) ◽  
pp. 412-415 ◽  
Author(s):  
Agustín Hernández ◽  
David T. Cooke ◽  
David T. Clarkson
Keyword(s):  
Plasma Membrane ◽  
Western Blot ◽  
Blot Analysis ◽  
Proton Transport ◽  
Western Blot Analysis ◽  
Ustilago Maydis ◽  
Hydrolytic Activity ◽  
Polypeptide Pattern

ABSTRACT Accumulation of 14α-methylated sterols or Δ8-sterols in Ustilago maydis affected three aspects of the plasma membrane H+-ATPase. Proton transport was reduced in Δ8-sterol-accumulating samples, due to an altered H+/ATP stoichiometry. ATP hydrolytic activity was increased, but no direct correlation with the extent or type of abnormal sterol accumulated could be drawn. Finally, Western blot analysis with antibodies against yeast PMA1 revealed a second lighter band (99-kDa band) in all samples from abnormal-sterol-accumulating sporidia. The conclusions are that the 99-kDa band and a reduced stoichiometry are directly linked to the presence of abnormal sterols, while changes in hydrolytic activity are linked only indirectly.

scholarly journals Electrogenic proton transport in the plasma membrane of Neurospora

1975 ◽  
Vol 15 (9) ◽  
pp. 968-971 ◽  
Author(s):  
C.L. Slayman ◽  
D. Gradmann
Keyword(s):  
Plasma Membrane ◽  
Proton Transport

Regulation of proton transport in urinary epithelia

1983 ◽  
Vol 106 (1) ◽  
pp. 135-141 ◽  
Author(s):  
Q. Al-Awqati ◽  
S. Gluck ◽  
W. Reeves ◽  
C. Cannon
Keyword(s):  
Plasma Membrane ◽  
Substrate Specificity ◽  
Proton Transport ◽  
Transport Activity ◽  
Kidney Medulla ◽  
F1 Atpase ◽  
Yeast Plasma Membrane ◽  
Luminal Membrane ◽  
Turtle Bladder ◽  
Proton Translocating Atpase

In urinary epithelia, like the turtle bladder, protons are transported by a H+ translocating ATPase located in the luminal membrane. We have recently discovered that the H+ pump is stored in small vesicles that lie underneath the luminal membrane. CO2, a major regulator of H+ transport causes these vesicles to fuse with the membrane thereby inserting more H+ pumps. We have now isolated these vesicles from the turtle bladder and from beef kidney medulla. Based on inhibitor sensitivity and substrate specificity this proton translocating ATPase is different from the mitochondrial F0-F1 ATPase, yeast plasma membrane and the gastric H+,K+-ATPase. Solubilization and reconstitution of the enzyme into liposomes shows retention of transport activity and inhibitor sensitivity.

Sign in / Sign up

Export Citation Format

Share Document