title: Nucleoside triphosphatase from the hen's egg white and vitelline membrane: purification, properties and relation to similar enzymes from the oviduct.
abstract: Hen's egg white and vitelline membrane nucleoside triphosphatases were purified resulting in active soluble subunits with MR 260,000 +/- 10,000. PH optima are divalent cation dependent and situated at pH 6.2 and 8.0 with ATP and at pH 6.15 with ADP as substrate. Ca2+ and Mg2+ are activators. Km and Ki values for Pi and PPi were determined. The enzymes are specific neither for ATP nor for ADP alone. No separation between nucleoside triphosphatase and nucleoside diphosphatase could be achieved. Differences found in their action can be due to differences in organization and properties of the (intermediary) enzyme-substrate complexes. A close relationship exists with homologous enzymes found in oviductal secretory cells and in oviductal secretions.
mesh_terms: D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002413:Cations, Divalent; D002645:Chickens; D011756:Diphosphates / Q000494:pharmacology; D005260:Female; D008970:Molecular Weight; D010063:Ovum / Q000201:enzymology*; D013379:Substrate Specificity; D014817:Vitelline Membrane / Q000201:enzymology*
chemical_list: D002413:Cations, Divalent; D011756:Diphosphates; D000251:Adenosine Triphosphatases