scholarly journals Characterization of a Partially Purified Adenosine Triphosphatase from a Corn Root Plasma Membrane Fraction

1981 ◽  
Vol 67 (1) ◽  
pp. 59-63 ◽  
Author(s):  
Frances M. Dupont ◽  
Linda L. Burke ◽  
Roger M. Spanswick
Keyword(s):  
Plasma Membrane ◽  
Membrane Fraction ◽  
Adenosine Triphosphatase ◽  
Corn Root ◽  
Plasma Membrane Fraction ◽  
Root Plasma Membrane

scholarly journals Preparation and Characterization of a Hormone-responsive Renal Plasma Membrane Fraction

1972 ◽  
Vol 247 (21) ◽  
pp. 6913-6918 ◽  
Author(s):  
Stephen J. Marx ◽  
Susan A. Fedak ◽  
G.D. Aurbach
Keyword(s):  
Plasma Membrane ◽  
Membrane Fraction ◽  
Plasma Membrane Fraction

Characterization of plasma membrane fraction from filamentous fungus Rhizopus nigricans

2000 ◽  
Vol 439 (7) ◽  
pp. R137-R138
Author(s):  
Helena Lenasi ◽  
Maja Šlajpah ◽  
Maksimiljan Sterle ◽  
Tamara Hudnik-Plevnik ◽  
Katja Breskvar
Keyword(s):  
Plasma Membrane ◽  
Filamentous Fungus ◽  
Membrane Fraction ◽  
Rhizopus Nigricans ◽  
Plasma Membrane Fraction

Isolation and characterization of plasma membranes from bovine carotid arteries

1986 ◽  
Vol 250 (1) ◽  
pp. C65-C75 ◽  
Author(s):  
R. V. Sharma ◽  
R. C. Bhalla
Keyword(s):  
Plasma Membrane ◽  
Cytochrome C ◽  
Membrane Fraction ◽  
Plasma Membranes ◽  
Carotid Arteries ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Cytochrome C Reductase ◽  
Plasma Membrane Fraction

A plasma membrane fraction from bovine carotid arteries has been isolated by extraction of a crude microsomal fraction with a low-ionic-strength buffer containing ATP and Ca2+. This step was followed by sucrose-density-gradient centrifugation in the presence of 0.6 M KCl. The plasma membrane vesicles were enriched 60- to 80-fold in Na+-K+-adenosinetriphosphatase, 5'-nucleotidase, and phosphodiesterase I activities. The final yields of these marker enzymes were 12-18% of the total activities in the postnuclear supernatant, and the protein yield was 100-120 micrograms/g wet wt of carotid arteries. Contamination of the plasma membrane fraction by mitochondria and sarcoplasmic reticulum was low as judged by low activities of succinate--cytochrome-c reductase and NADPH--cytochrome-c reductase, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation with smooth muscle-specific actin antibodies showed that the plasma membrane fraction was substantially free from myosin and actin contamination. The plasma membrane vesicles accumulated Ca2+ in the presence of ATP, and the accumulation was increased by calmodulin. Ca2+ accumulated in the presence or absence of calmodulin could be released almost completely from the vesicles by the addition of the Ca2+ ionophore A23187 but not by ethyleneglycol-bis(beta-aminoethylether)-N,N'-tetraacetic acid, indicating that Ca2+ uptake in the presence of ATP is intravesicular. The effects of phosphate and oxalate on Ca2+ uptake in the plasma membranes were different from one another. Phosphate increased Ca2+ uptake in a concentration- and time-dependent manner, and the increase in Ca2+ uptake could be observed as early as 1 min. On the other hand, oxalate at concentrations up to 5 mM did not increase Ca2+ uptake significantly during the 30-min incubation. These plasma membranes can prove useful for the study of ion transport across plasma membranes, hormone binding, characterization of calcium channels, and preparation of antibodies against plasma membrane proteins.

Preparation and characterization of a plasma-membrane fraction isolated from sheep parotid glands

1990 ◽  
Vol 18 (4) ◽  
pp. 646-646
Author(s):  
STEVEN VAYRO ◽  
SORAYA SHIRAZI-BEECHEY ◽  
RICHARD KEMP ◽  
R. BRIAN BEECHEY
Keyword(s):  
Plasma Membrane ◽  
Membrane Fraction ◽  
Parotid Glands ◽  
Plasma Membrane Fraction ◽  
Sheep Parotid
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