scholarly journals Partial characterization of a phosphorylated intermediate associated with the plasma membrane ATPase of corn roots

1982 ◽  
Vol 79 (22) ◽  
pp. 6922-6926 ◽  
Author(s):  
D. P. Briskin ◽  
R. T. Leonard
Keyword(s):  
Plasma Membrane ◽  
Partial Characterization ◽  
Plasma Membrane Atpase ◽  
Corn Roots ◽  
Membrane Atpase

scholarly journals Secretory vesicles externalize the major plasma membrane ATPase in yeast.

1988 ◽  
Vol 106 (3) ◽  
pp. 641-648 ◽  
Author(s):  
C L Holcomb ◽  
W J Hansen ◽  
T Etcheverry ◽  
R Schekman
Keyword(s):  
Plasma Membrane ◽  
Secretory Pathway ◽  
Biochemical Characterization ◽  
Plasma Membrane Atpase ◽  
Membrane Assembly ◽  
Yeast Cell Surface ◽  
Membrane Atpase ◽  
Constitutive Secretion ◽  
Secretory Enzyme

Yeast cell surface growth is accomplished by constitutive secretion and plasma membrane assembly, culminating in the fusion of vesicles with the bud membrane. Coordination of secretion and membrane assembly has been investigated by examining the biogenesis of plasma membrane ATPase (PM ATPase) in secretion-defective (sec) strains of Saccharomyces cerevisiae. PM ATPase is synthesized as a approximately 106-kD polypeptide that is not detectably modified by asparagine-linked glycosylation or proteolysis during transit to the plasma membrane. Export of the PM ATPase requires the secretory pathway. In sec1, a mutant defective in the last step of secretion, large amounts of Golgi-derived vesicles are accumulated. Biochemical characterization of this organelle has demonstrated that PM ATPase and the secretory enzyme, acid phosphatase, are transported in a single vesicle species.

scholarly journals The vanadate-sensitive ATPase from plasma membrane of maize roots

2014 ◽  
Vol 62 (3-4) ◽  
pp. 171-173
Author(s):  
Tatiana Pšenáková ◽  
Slavomira Kašiarová
Keyword(s):  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Plasma Membrane Atpase ◽  
Plasma Membrane Vesicles ◽  
Temperature Optimum ◽  
Corn Roots ◽  
Phospholipid Liposomes ◽  
Maize Roots ◽  
Membrane Atpase ◽  
Soybean Phospholipid

Plasma membrane vesicles isolated from corn roots were shown to possess Mg<sup>2+</sup>- dependent and K<sup>+</sup> - stimulated ATPase activity, which was inhibited by vanadate, insensitive to nitrate and molybdate, and very little sensitive to azide. The optimum of phosphohydrolase activity was at pH 6.5 and temperature optimum 40<sup>o</sup>C. ATP was the preferred substrate. The Plasma membrane ATPase was reconstituted into soybean phospholipid liposomes.

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