Partial Purification and Characterization of An ATPase in Mung Bean Hypocotyl Plasma Membrane: Suggestion for A New Type of Higher Plant Plasma Membrane ATPase

1988 ◽  
Keyword(s):  
Plasma Membrane ◽  
Partial Purification ◽  
Plasma Membrane Atpase ◽  
Higher Plant ◽  
Membrane Atpase ◽  
Bean Hypocotyl ◽  
New Type ◽  
Plant Plasma Membrane ◽  
Mung Bean Hypocotyl

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.

Reconstitution and rapid partial purification of the red beet plasma membrane ATPase

1987 ◽  
Vol 69 (4) ◽  
pp. 617-626 ◽  
Author(s):  
Sashi P. Singh ◽  
B. V. Sudershan Kesav ◽  
Donald P. Briskin
Keyword(s):  
Plasma Membrane ◽  
Partial Purification ◽  
Plasma Membrane Atpase ◽  
Red Beet ◽  
Membrane Atpase
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