A "Reagentless" Fluorometric Method for Creatine Kinase Activity in Serum

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A "reagentless" fluorometric method for creatine kinase activity in serum.

Measurement of serum creatine kinase (CK; EC 2.7.3.2) activity is of great value in the diagnosis of myocardial and skeletal muscle diseases (1-3). The greater specificity of CK over that of other enzymes, such as lactate dehydrogenase and aspartate aminotransferase, for the detection of muscular dystrophy and myocardial infarction has attracted much interest in CK determinations. In a prelimin...

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Fluorometric measurement of creatine kinase activity.

SERUM CREATINE KINASE activity has beell measured by determining the amount of creatine liberated in the following reaction: ADI + creatine phosphate ATP + creatine. The Voges-Proskauer reactioii, production of a color by reaction of creatille with diacetyl alid -naphthol, has heeii used to measure enzymatically released creatine (1-5). The presence of a sulfhydryl compound in tile incubatioii ...

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Automated method for the determination of serum creatine kinase activity.

An automated (AutoAnalyzer) method for the colorimetric determination of creatine kinase activity in serum is described. This method includes reactivation of creatine kinase with cysteine, incubation of the active enzyme with creatine phosphate and adenosine diphosphate at 3750, and subsequent inactivation of enzyme and binding of csteine by phenylmercuric borate. The enzymatically produced cre...

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Fluorometric method for measuring serum lipase activity.

We describe a method for determining lipase (triacylglycerol acyl-hydrolase, EC 3.1.1.3) activity in serum. Emulsified olive oil in tris(hydroxymethyl)aminomethane buffer is used as substrate. The course of the enzymatic reaction is followed by measuring the decrease in fluorescence with time of a fluorescent indicator, 4-methylumbelliferone, added to the substrate, caused by the change in the ...

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Observations on the fluorometric measurement of creatine kinase activity.

Twenty patients’ serums have been analyzed by both the Sax-Moore (1) and ConnAnido (2) creatine kinase methods. No significant difference in enzyme activity was found. In our hands, the Conn-Anido procedure, as originally described, gave variable results and high background fluorescence. The presence of high alkaline or acid phosphataseactivities in specimensanalyzed by the Sax-Moore procedure ...

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ژورنال

عنوان ژورنال: Clinical Chemistry

سال: 1973

ISSN: 0009-9147,1530-8561

DOI: 10.1093/clinchem/19.9.1045