Creatine Kinase Isoenzymes: Electrophoretic and Quantitative Measurements

Foreback, Craig C.; Chu, J W

doi:10.3109/10408368109105871

Cited by 10 publications

(13 citation statements)

References 209 publications

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“…It is well-known that in the electrophoretic method the fluorescence at higher intensity is quenched (2,11). As the creatine kinase-MM fraction is always greater than the creatine kinase-MB fraction this will cause overestimation of creatine kinase-MB activity (11).…”

Section: Discussionmentioning

confidence: 99%

“…Serum samples were diluted at total creatine kinase activities above 1400 U/l. Relative creatine kinase-MB activity was measured by fluorometry, using a Vitatron TLD 100 densitometer (Vitatron, Dieren, The Netherlands) after electrophoretic separation on agarose gel film and reaction with substrate (Creatine Phosphokinase Isoenzyme Substrate SetComing, Halstead, UK) (2,3). By this method the creatine kinase is separated into the three main isoenzymes: creatine kinase-MM, creatine kinase-MB, and creatine kinase-BB.…”

Section: Electrophoretic Methodsmentioning

confidence: 99%

“…The serum sample was kept at -80 °C until assayed. 2 ) n: number of observations r: correlation coefficient SD: standard deviation SEE: standard error of estimate n. s.: non significant Tab. 1.…”

Section: ) Precisionmentioning

confidence: 99%

“…The aim of this specific diagnostic test. The most widely used single study is to compare two different immunoinhibition laboratory test is electrophoretic determination of the methods (a dry and a wet chemistry method) with the MB isoenzyme of creatine kinase (EC 2.7.3.2) 1 ) (crea-commonly used but laborious electrophoretic method, tine kinase-MB) (1,2). This method is very specific and reasonably sensitive, but it is rather tedious and expensive (3,4).…”

Section: Introductionmentioning

confidence: 99%

“…, specific antibodies against the subumt M. The antiAcute myocardial infarction is one of the commonest bodies have either been used in radioimmunoassays causes of hospitalization and death in the western or for specific inhibition of the enzymatic activity of industrialized countries. It is therefore of great im-the subunit M, followed by measurement of the reportance to have a fast, inexpensive, sensitive, and maining enzymatic activity (2,5). The aim of this specific diagnostic test.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of Two Immunoinhibitory Methods with Agarose Gel-Electrophoresis for Measuring the MB Isoenzyme of Creatine Kinase in Serum from Cases of Suspected Myocardial Infarction

Hadberg¹,

Hassager²,

Hildebrandt³

et al. 1990

Clinical Chemistry and Laboratory Medicine

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Summary:Two immunoinhibitory methods for measuring creatine kinase-MB (a dry chemical and a wet chemical method) were compared with the commonly used agarose gel electrophoretic method, using 563 serum samples from 235 patients with suspected acute myocardial infarction. Comparison of the electrophoretic and the dry chemistry methods showed the linear relationship: electrophoretic method = -6.5 U/l + 1.22 χ dry chemistry method, r = 0.943. For the wet chemistry method the relationship was: electrophoretic method = -7.2 U/l + 1.19 x wet chemistry method, r = 0.854. Parallel determinations of total creatine kinase were also done and the methods were virtually identical in performance.Compared with the electrophoretic method (which showed a 15% prevalence of acute myocardial infarction), these classifications showed sensitivities of 0.92 and 0.67 and specificities of 0.94 and 0.99 (dry and wet chemistry, respectively; using methods recommended by the manufacturers). After optimization of discriminators the sensitivity was increased to 0.94/0.92 and the specificity to 0.99/0.99. Introduction." ., ,. . , specific antibodies against the subumt M. The antiAcute myocardial infarction is one of the commonest bodies have either been used in radioimmunoassays causes of hospitalization and death in the western or for specific inhibition of the enzymatic activity of industrialized countries. It is therefore of great im-the subunit M, followed by measurement of the reportance to have a fast, inexpensive, sensitive, and maining enzymatic activity (2, 5). The aim of this specific diagnostic test. The most widely used single study is to compare two different immunoinhibition laboratory test is electrophoretic determination of the methods (a dry and a wet chemistry method) with the MB isoenzyme of creatine kinase (EC 2.7.3.2) 1 ) (crea-commonly used but laborious electrophoretic method, tine kinase-MB) (1, 2). This method is very specific and reasonably sensitive, but it is rather tedious and expensive (3, 4). The last decade has seen the devel-Materials and Methods opment of easier analytical methods, which utilize Samples

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Section: Discussionmentioning

confidence: 99%

Section: Electrophoretic Methodsmentioning

confidence: 99%

Section: ) Precisionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Comparison of Two Immunoinhibitory Methods with Agarose Gel-Electrophoresis for Measuring the MB Isoenzyme of Creatine Kinase in Serum from Cases of Suspected Myocardial Infarction

Hadberg¹,

Hassager²,

Hildebrandt³

et al. 1990

Clinical Chemistry and Laboratory Medicine

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Creatine Kinase Isoenzymes and Prostatic Carcinoma: Metastatic Disease or Acute Myocardial Infarction?

Stein

Dalal

1984

Journal of Urology

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The measurement of creatine kinase isoenzymes, particularly the MB fraction, is a major determinant for acute myocardial infarction. Patients with metastatic carcinoma of the prostate may have an elevated serum creatine kinase-BB fraction, which by some automated laboratory techniques may be read mistakenly as creatine kinase-MB. We report such a case and discuss the creatine kinase isoenzyme measurement.

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Creatine kinase activity and isoenzymes in lung, colon and liver carcinomas

Joseph

Cardesa²,

Carreras³

1997

Br J Cancer

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SummaryWe have compared the levels of creatine kinase (CK) activity and the distribution of CK isoenzymes determined by agarose gel electrophoresis in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinomas, lung squamous cell carcinomas and lung carcinoids. Colon and lung adenocarcinomas, and squamous cell carcinomas presented lower CK activity than the normal tissues and no differences were found between hepatocarcinoma and normal liver tissue. In contrast, lung carcinoids had higher CK activity than normal lung tissue. Type BB-CK was the predominant isoenzyme in normal lung, colon and liver tissues. Type MM isoenzyme was detected in normal lung and type MB-CK was found in normal colon. In most lung tumours the CK isoenzyme electrophoretic pattern did not change. However, no type BB-CK was detected in some hepatocarcinomas, type MM-CK decreased in lung carcinoids and type MB isoenzyme was not observed in colon adenocarcinomas. It is concluded that in most tumours there is a decrease in the expression of type B-and type M-CK subunits, whereas in lung carcinoid the expression of type B-CK activity increases. Thus, the increase in type BB-CK observed in the serum of patients with lung and colon adenocarcinomas is probably due mainly to enhanced enzyme release as a result of tumour cell necrosis.

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Creatine Kinase Isoenzymes: Electrophoretic and Quantitative Measurements

Cited by 10 publications

References 209 publications

Comparison of Two Immunoinhibitory Methods with Agarose Gel-Electrophoresis for Measuring the MB Isoenzyme of Creatine Kinase in Serum from Cases of Suspected Myocardial Infarction

Comparison of Two Immunoinhibitory Methods with Agarose Gel-Electrophoresis for Measuring the MB Isoenzyme of Creatine Kinase in Serum from Cases of Suspected Myocardial Infarction

Creatine Kinase Isoenzymes and Prostatic Carcinoma: Metastatic Disease or Acute Myocardial Infarction?

Creatine kinase activity and isoenzymes in lung, colon and liver carcinomas

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