scholarly journals Phosphorylation of the Adenosine Triphosphatase in a Deoxycholate-Treated Plasma Membrane Fraction from Corn Roots

1982 ◽  
Vol 70 (5) ◽  
pp. 1459-1464 ◽  
Author(s):  
Donald P. Briskin ◽  
Robert T. Leonard
Keyword(s):  
Plasma Membrane ◽  
Membrane Fraction ◽  
Adenosine Triphosphatase ◽  
Plasma Membrane Fraction ◽  
Corn Roots

scholarly journals Plasma membrane of the rat parotid gland: preparation and partial characterization of a fraction containing the secretory surface.

1982 ◽  
Vol 95 (1) ◽  
pp. 8-19 ◽  
Author(s):  
P Arvan ◽  
J D Castle
Keyword(s):  
Plasma Membrane ◽  
Parotid Gland ◽  
Membrane Fraction ◽  
Adenosine Triphosphatase ◽  
Plasma Membranes ◽  
Junctional Complex ◽  
Salivary Gland Cell ◽  
Plasma Membrane Fraction ◽  
Rat Parotid Gland ◽  
Rat Parotid

A plasma membrane fraction from the rat parotid gland has been prepared by a procedure which selectively enriches for large membrane sheets. This fraction appears to have preserved several ultrastructural features of the acinar cell surface observed in situ. Regions of membrane resembling the acinar luminal border appear as compartments containing microvillar invaginations, bounded by elements of the junctional complex, and from which basolateral membranes extend beyond the junctional complex either to contact other apical compartments or to terminate as free ends. Several additional morphological features of the apical compartments suggest that they are primarily derived from the surface of acinar cells, rather than from the minority of other salivary gland cell types. Enzymatic activities characteristically associated with other cellular organelles are found at only low levels in the plasma membrane fraction. The fraction is highly enriched in two enzyme activities--K+ -dependent p-nitrophenyl phosphatase (K+ -NPPase, shown to be Na+/K+ adenosine triphosphatase; 20-fold) and gamma-glutamyl transpeptidase (GGTPase; 26-fold)--both known to mark plasma membranes in other tissues. These activities exhibit different patterns of recovery during fractionation, suggesting their distinct distributions among parotid cellular membranes. Secretion granule membranes also exhibit GGTPase, but no detectable K+ -NPPase. Since Na+/K+ adenosine triphosphatase and GGTPase, respectively, mark the basolateral and apical cellular surfaces in other epithelia, we hypothesize that these two enzymes mark distinct domains in the parotid plasmalemma, and that GGTPase, as the putative apical marker, may signify a compositional overlap between the two types of membranes which fuse during exocytosis.

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