Bioluminescence flow sensor for determination of creatine kinase activity in blood

1989 ◽  
Vol 227 ◽  
pp. 29-36 ◽  
Author(s):  
S. Girotti ◽  
M.L. Cascione ◽  
S. Ghini ◽  
G. Carrea ◽  
R. Bovara ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Flow Sensor

scholarly journals FLUORIMETRIC DETERMINATION OF CREATINE KINASE ACTIVITY IN ISOLATED SINGLE NEURONS

1973 ◽  
Vol 21 (6) ◽  
pp. 568-571 ◽  
Author(s):  
IGOR B. KRASNOV
Keyword(s):  
Creatine Kinase ◽  
Enzyme Activity ◽  
Coefficient Of Variation ◽  
Kinase Activity ◽  
Tissue Sample ◽  
Vestibular Nucleus ◽  
Creatine Kinase Activity ◽  
Single Neurons ◽  
Fluorimetric Determination

A quantitative fluorimetric method for determination of creatine kinase activity in isolated single nerve cells (2-10 ng dry weight) has been developed. Enzyme activity was measured in the direction of adenosine triphosphate and creatine formation. The creatine generated was measured by the fluorescent compound formed with ninhydrin in alkali. The coefficient of variation for the assay of enzyme activity in brain homogenate (47 ng wet tissue/sample) was 3.17%. The coefficient of variation for single neurons of the lateral vestibular nucleus (nucleus Deitersi) in rabbit was about 15%. The creatine kinase activity in these cell bodies was 342.0 ± 14.2 moles/kg dry tissue/hr, at 38°C.

Evaluation of a New Procedure for Measuring Serum Creatine Kinase Activity

1970 ◽  
Vol 16 (5) ◽  
pp. 370-374 ◽  
Author(s):  
J Henry Wilkinson ◽  
B Steciw
Keyword(s):  
Creatine Kinase ◽  
Spectrophotometric Method ◽  
Kinase Activity ◽  
Creatine Phosphate ◽  
Sample Volume ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Normal Range ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract A new spectrophotometric microtechnique for the determination of serum creatine kinase activity, in which all reagents are provided in a single com-pressed tablet, has been evaluated. The procedure depends upon coupling the creatine phosphate-ADP reaction with the hexokinase and glucose-6-phosphate dehydrogenase reactions. The new technique is quick, relatively simple, and gives results which compare favorably with the conventional spectrophotometric method in precision and sensitivity. It requires a sample volume of 10 Al, and values ranging from 10 to1600 U/liter can be determined without dilution. Gross hemolysis leads to erroneously high values, but the error is negligible with slightly hemolyzed specimens. A provisional normal range has been established

Automated Method for the Determination of Serum Creatine Kinase Activity

1967 ◽  
Vol 13 (3) ◽  
pp. 233-241 ◽  
Author(s):  
Gerard A Fleisher
Keyword(s):  
Creatine Kinase ◽  
Alkaline Solution ◽  
Kinase Activity ◽  
Adenosine Diphosphate ◽  
Creatine Phosphate ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Colorimetric Determination ◽  
Automated Method

Abstract 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 37.5°, and subsequent inactivation of enzyme and binding of cysteine by phenylmercuric borate. The enzymatically produced creatine is dialyzed against a solution of diacetyl and reacted with α-naphthol in an alkaline solution. The absorbance of the colored end product is measured at 550 mµ. Individual blanks are determined in the absence of adenosine diphosphate. Comparison of results obtained by this method and a manual procedure shows satisfactory agreement.

Automated determination of creatine kinase activity in serum with use of thermostable glucokinase

1991 ◽  
Vol 37 (3) ◽  
pp. 452-454
Author(s):  
Ikuhiro Maeda ◽  
Sadao Hayashi ◽  
Nobuyuk Amino ◽  
Kiyosh Miyai
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Clinical Chemistry ◽  
German Society ◽  
Creatine Kinase Activity ◽  
Manual Method ◽  
Biochemical Analyzer ◽  
Automated Determination ◽  
Better Than

Abstract We measured creatine kinase (CK, EC 2.7.3.2) activity in serum with a new reagent system utilizing thermostable glucokinase (EC 2.7.1.2). Automated determinations were performed with Toshiba's Model TBA-80S Biochemical Analyzer. Precision studies demonstrated within-run and between-run CVs of 0.4%-2.4% and 2.8%-3.1%, respectively. The response linearity was confirmed for CK activity up to 1000 U/L at 37 degrees C. CK activities correlated well (r = 0.997) with those obtained by the manual method recommended by the German Society for Clinical Chemistry (measuring at 37 degrees C) involving hexokinase (EC 2.7.1.1). However, CK activities measured by our method were consistently higher than those of the hexokinase method at reaction temperatures of 30, 37, and 40 degrees C. These data indicate that the new method with thermostable glucokinase is better than that with thermo-unstable hexokinase for determination of CK activity in serum.

Adenylate kinase inhibition by adenosine 5'-monophosphate and fluoride in the determination of creatine kinase activity.

1978 ◽  
Vol 24 (3) ◽  
pp. 498-501 ◽  
Author(s):  
F Meiattini ◽  
G Giannini ◽  
P Tarli
Keyword(s):  
Creatine Kinase ◽  
Adenylate Kinase ◽  
Kinase Activity ◽  
Clinical Chemistry ◽  
German Society ◽  
Significant Loss ◽  
Creatine Kinase Activity ◽  
Low Concentrations ◽  
Diadenosine Pentaphosphate

Abstract The current methods for the determination of creatine kinase (EC 2.7.3.2) activity are derived from Oliver's method, in which AMP is used to decrease interference by adenylate kinase (EC 2.7.4.3). Recently, Szasz et al. and Rosano et al. described methods in which diadenosine pentaphosphate and fluoride, respectively, are used to reduce this interference. However, diadenosine pentaphosphate does not sufficiently inhibit such activity of hepatic origin, while fluoride alone can only inhibit it at concentrations at which the fluoride tends to precipitate as MgF2. Finally, Szasz et al., the Committee on Enzymes of the Scandinavian Society for Clinical Chemistry and Clinical Physiology, and the German Society for Clinical Chemistry have proposed methods in which both AMP and diadenosine pentaphosphate are used to inhibit adenylate kinase. We have found that by using low concentrations of AMP and fluoride together, we can greatly diminish this interference without significant loss of creatine kinase activity and with no precipitation of MgF2.

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