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Literature DB >> 3156588

Presence of a high-affinity Ca2+- and Mg2+-dependent ATPase in rat peritoneal mast-cell membranes.

Abstract

Purified perigranular and plasma membranes isolated from rat peritoneal mast cells were examined for Ca2+- and Mg2+-dependent ATPase activity. Isolated perigranular membranes contained only a low-affinity Ca2+- or Mg2+-dependent ATPase (Km greater than 0.5 mM). The plasma membranes contained both a low-affinity Ca2+- or Mg2+-dependent ATPase (Km = 0.4 mM, Vmax. = 20 nmol of Pi/min per mg), as well as a high-affinity Ca2+- and Mg2+-dependent ATPase (Km = 0.2 microM, Vmax. = 6 nmol of Pi/min per mg).

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Year: 1985 PMID： 3156588 PMCID： PMC1144711 DOI： 10.1042/bj2260335

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

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References

13 in total

1. Ca2+-Mg2+-activated adenosine triphosphatase in plasma and granule membranes in non-secreting and secreting mast cells.

Authors: N Chakravarty; E H Nielsen
Journal: Exp Cell Res Date: 1980-11 Impact factor: 3.905

2. Plasma membrane adenosine triphosphatases in rat peritoneal mast cells and macrophages--the relation of the mast cell enzyme to histamine release.

Authors: N Chakravarty; Z Echetebu
Journal: Biochem Pharmacol Date: 1978 Impact factor: 5.858

Presence of a high-affinity Ca2+- and Mg2+-dependent ATPase in rat peritoneal mast-cell membranes.

1. Ca2+-Mg2+-activated adenosine triphosphatase in plasma and granule membranes in non-secreting and secreting mast cells.

2. Plasma membrane adenosine triphosphatases in rat peritoneal mast cells and macrophages--the relation of the mast cell enzyme to histamine release.

3. A semi-automated method for the determination of multiple membrane ATPase activities.

4. Isolation of rat mast cell granules with intact membranes.

5. A simplification of the protein assay method of Lowry et al. which is more generally applicable.

6. Effect of sulfhydryl-reactive ATPase inhibitors upon mast cell and basophil activation.

7. Characterization of the Ca2+- and Mg2+-dependent ATPases in Electrophorus electroplax microsomes.

8. Modulation of cyclic AMP in purified rat mast cells. I. Responses to pharmacologic, metabolic, and physical stimuli.

9. Ethacrynic acid inhibitable Ca2+ and Mg2+-activated membrane adenosine triphosphatase in rat mast cells.

10. Characterization of calcium-ion-activated adenosine triphosphatase in the plasma membrane of rat mast cells.