Effect of Salt and Substrate Concentration upon Activity of Adenosinetriphosphatase

Autor:	John W. Mehl, Edwin L. Sexton
Rok vydání:	1943
Předmět:	chemistry.chemical_classification biology Chemistry ATPase Inorganic chemistry Salt (chemistry) Phosphate Substrate concentration General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Enzyme Glycine biology.protein Linear rate
Zdroj:	Experimental Biology and Medicine. 52:38-40
ISSN:	1535-3699 1535-3702
DOI:	10.3181/00379727-52-14014
Popis:	SummaryMeasurement of the activity of ATP-ase in salt concentrations from 0.15 to 0.55 M show that the activity is decreased as the KC1 concentration increases. The magnitude of the effect depends upon pH and the presence or absence of glycine. The rate of formation of inoranic phosphote is also found to be independent of the substrate concentration when the ATP concentration is 0.23 mM per liter or greater. Observed deviations from a linear rate of formation of phosphate at the higher ATP concentration must be attributed to inactivation of the enzyme during the course of the experiment.
Databáze:	OpenAIRE
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