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.

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

Creatine kinase response surfaces explored by use of factorial experiments and simplex maximization.

1983 ◽  
Vol 29 (5) ◽  
pp. 793-799 ◽  
Author(s):  
D M Fast ◽  
E J Sampson ◽  
V S Whitner ◽  
M Ali
Keyword(s):  
Creatine Kinase ◽  
Response Surface ◽  
Kinase Activity ◽  
Adenosine Diphosphate ◽  
Creatine Phosphate ◽  
Creatine Kinase Activity ◽  
Response Surfaces ◽  
Optimal Conditions ◽  
Reaction Conditions ◽  
Sensitivity Reaction

Abstract We conducted a five-component, five-level response-surface experiment to optimize the pH and the concentrations of magnesium, creatine phosphate, adenosine diphosphate, and buffer in an assay for creatine kinase. Under optimal conditions, creatine kinase activity was about 5% greater than that obtained with a previously reported assay (Clin Chem 23: 1569, 1977). We also applied a simplex maximization algorithm to the response-surface equation to locate areas of maximum sensitivity. Reaction conditions for two such areas were found, each yielding approximately 11% more activity than with the previously reported method.

Distribution of serum creatine kinase activity in young healthy persons

1999 ◽  
Vol 279 (1-2) ◽  
pp. 107-115 ◽  
Author(s):  
Eli I. Lev ◽  
Ilan Tur-Kaspa ◽  
Isaac Ashkenazy ◽  
Anat Reiner ◽  
David Faraggi ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Healthy Persons

Skeletal muscle collagen content in humans after high-force eccentric contractions

2004 ◽  
Vol 97 (1) ◽  
pp. 197-203 ◽  
Author(s):  
Abigail L. Mackey ◽  
Alan E. Donnelly ◽  
Taina Turpeenniemi-Hujanen ◽  
Helen P. Roper
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Staining Intensity ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Muscle Contractions ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Eccentric Contractions ◽  
Knee Extensors ◽  
Type Iv

The purpose of this study was to investigate the effects of high-force eccentric muscle contractions on collagen remodeling and on circulating levels of matrix metalloproteinases (MMP) and tissue inhibitors of metalloproteinases (TIMP) in humans. Nine volunteers [5 men and 4 women, mean age 23 (SD 4) yr] each performed a bout of 100 maximum voluntary eccentric contractions of the knee extensors. Muscle biopsies were taken before exercise and on days 4 and 22 afterward. Image analysis of stained tissue sections was used to quantify endomysial collagen staining intensity. Maximum voluntary contractile isometric force was recorded preexercise and on days 1, 2, 3, 4, 8, 11, and 14 postexercise. Venipuncture blood samples were also drawn on these days for measurement of serum creatine kinase activity and concentrations of MMP-9, TIMP-1, TIMP-2, and the MMP-2/TIMP-2 complex. Maximum voluntary contractile force declined by 39 ± 23% (mean ± SD) on day 2 postexercise and recovered thereafter. Serum creatine kinase activity peaked on day 4 postexercise ( P < 0.01). Collagen type IV staining intensity increased significantly on day 22 postexercise to 126 ± 29% (mean ± SD) of preexercise values ( P < 0.05). Serum MMP-9 levels increased on day 8 postexercise ( P < 0.01), and serum TIMP-1 was also significantly elevated on days 1, 2, 3, 4, and 14 postexercise ( P < 0.05). These results suggest that a single bout of eccentric muscle contractions results in remodeling of endomysial type IV collagen, possibly via the MMP pathway.

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

1973 ◽  
Vol 19 (9) ◽  
pp. 1045-1048 ◽  
Author(s):  
Herbert K Y Lau ◽  
George G Guilbault
Keyword(s):  
Creatine Kinase ◽  
Silicone Rubber ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Fluorometric Method ◽  
Nadh Fluorescence

Abstract A "reagentless" fluorometric method is described for the analysis of serum creatine kinase (CK) activity. The method is based on the use of silicone rubber pads, upon which are placed all the reagents for assay of CK. The rate of formation of NADH fluorescence at 460 nm is measured and equated to CK activity. The method is simple, rapid, inexpensive, and as little as 3 µl of serum is needed.

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

Evaluation of adenosine 5'-monophosphate and fluoride as adenylate kinase inhibitors in the creatine kinase assay.

1976 ◽  
Vol 22 (7) ◽  
pp. 1078-1083 ◽  
Author(s):  
T G Rosano ◽  
K J Clayson ◽  
P E Strandjord
Keyword(s):  
Creatine Kinase ◽  
Adenylate Kinase ◽  
Kinase Activity ◽  
Kinase Inhibitors ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Assay System ◽  
Kinase Assay ◽  
Rabbit Muscle ◽  
Atp Production

Abstract Adenylate kinase (EC 2.7.4.3) interferes positively in the serum creatine kinase (EC 2.7.3.2) assay when the rate of ATP production is monitored by a coupled enzyme system. A dual assay, measuring creatine kinase and adenylate kinase activity, was used to evaluate AMP and other possible adenylate kinase inhibitors that would permit specific measurement of creatine kinase activity in the presence of adenylate kinase. We found that AMP, routinely included in the creatine kinase assay system to inhibit adenylate kinase, partially inhibits both human serum creatine kinase and purified creatine kinase from rabbit muscle. The amount of creatine kinase inhibition is related directly to the AMP concentration and inversely to the substrate (ADP) concentration. We found that 25 mmol/liter of fluoride inhibits adenylate kinase without measurable effect on creatine kinase activity. We developed a serum creatine kinase assay including fluoride, and compared it with the dual assay system and with two commercial assay kits. Other halides or adenosine 2'-monophosphate did not selectively inhibit adenylate kinase.

Sign in / Sign up

Export Citation Format

Share Document