A fluorimetric method for continuously assaying ATPase: Application to small specimens of glycerol-extracted muscle fibers

A continuous fluorimetric method using auxiliary-coupling enzymes such as pyruvate kinase and lactate dehydrogenase for measuring ADP production to assay ATPase activity is described. This method is simpler, more rapid, and more sensitive than the previously used spectrophotometric method. The appli...

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Veröffentlicht in:Analytical biochemistry 1979-01, Vol.92 (2), p.375-382
Hauptverfasser: Takashi, Reiji, Putnam, Susan
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container_title Analytical biochemistry
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creator Takashi, Reiji
Putnam, Susan
description A continuous fluorimetric method using auxiliary-coupling enzymes such as pyruvate kinase and lactate dehydrogenase for measuring ADP production to assay ATPase activity is described. This method is simpler, more rapid, and more sensitive than the previously used spectrophotometric method. The application of this method for studying the ATPase of rabbit psoas muscle fibers during Mg 2+-ATP activation is also illustrated and discussed.
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subjects Adenosine Triphosphatases - analysis
Animals
Autoanalysis
Enzyme Activation
Glycerol
L-Lactate Dehydrogenase - pharmacology
Muscle Proteins - analysis
Muscles - enzymology
NAD - analysis
Pyruvate Kinase - pharmacology
Rabbits
Spectrometry, Fluorescence
title A fluorimetric method for continuously assaying ATPase: Application to small specimens of glycerol-extracted muscle fibers
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