Measurement of Brain-Specific Creatine Kinase Isoenzyme Activity in Serum

1975 ◽  
Vol 21 (11) ◽  
pp. 1663-1666 ◽  
Author(s):  
Daniel A Nealon ◽  
Arthur R Henderson
Keyword(s):  
Creatine Kinase ◽  
Serum Creatine Kinase ◽  
Brain Surgery ◽  
Chromatographic System ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Isoenzymes ◽  
Diethylaminoethyl Cellulose ◽  
Cellulose Column ◽  
Column Chromatographic

Abstract We further modified a diethylaminoethyl-cellulose column-chromatographic system [Clin. Chem. 21, 392 (1975)] so that it will separate all three serum creatine kinase isoenzymes. The modified system can be used to detect brain-specific creatine kinase isoenzyme in serum after brain surgery

Relative merits of two electrophoretic and two column-chromatographic kets for determining serum creatine kinase isoenzyme MB activity.

1978 ◽  
Vol 24 (11) ◽  
pp. 2013-2017 ◽  
Author(s):  
C Hamlin ◽  
E Ackerman
Keyword(s):  
Creatine Kinase ◽  
Clinical Evaluation ◽  
Serum Creatine Kinase ◽  
Cardiac Monitoring ◽  
Prospective Analysis ◽  
Creatine Kinase Isoenzyme ◽  
Discrepant Result ◽  
Column Chromatographic ◽  
Creatine Kinase Isoenzyme Mb

Abstract Prospective analysis (by use of commercially available kits) of 339 validated admission specimens from patients consecutively admitted to a cardiac monitoring unit revealed sensitivities of 68 and 63% for two electrophoretic assays (Bioware and Helena) and up to 73 and 77% for two chromatographic assays (Roche and Worthington). Specificities were 94.8, 96,6, 90.2, and 89.7% and efficiencies were 90.2, 90.7, 87.0, and 87.0, respectively. Although these results differ from early reports, they agree well with several recent studies. However, 86 (25%) of the specimens gave at least one discrepant result based on clinical evaluation of the patients, and 68 (20%) gave at least one discrepant result between methods.

Determination of serum creatine kinase isoenzymes in myocardial infarction

1972 ◽  
Vol 29 (6) ◽  
pp. 817-820 ◽  
Author(s):  
Aarne Konttinen ◽  
Hannu Somer
Keyword(s):  
Myocardial Infarction ◽  
Creatine Kinase ◽  
Serum Creatine Kinase ◽  
Creatine Kinase Isoenzymes

Improved separation of creatine kinase isoenzymes by use of DEAE-Sepharose Cl-6B.

1980 ◽  
Vol 26 (5) ◽  
pp. 618-624 ◽  
Author(s):  
R J Bondar ◽  
D G Shevchik ◽  
M Y Hsu ◽  
M M Kohler
Keyword(s):  
Creatine Kinase ◽  
Reference Interval ◽  
Serum Creatine Kinase ◽  
Cross Contamination ◽  
Column System ◽  
Bed Height ◽  
Creatine Kinase Isoenzymes ◽  
Sepharose Column ◽  
Coefficients Of Variation ◽  
Chromatographic Procedure

Abstract We describe here a simple, rapid chromatographic procedure for quantitatively separating serum creatine kinase isoenzymes (EC 2.7.3.2), with diethylaminoethyl (DEAE)-Sepharose CL-6B as the anion-exchanger. We established the column bed height and the elution parameters by use of a simplex procedure. DEAE-Sepharose CL-6B equilibrated in tris(hydroxymethyl)aminomethane (50 mmol/L, pH 7.5, and containing 30 mmol of NaCl per liter) is packed into a miniature polystyrene column with bed dimensions of 0.7 x 1.5 cm. The DEAE-Sepharose column system was evaluated and compared with a DEAE-Sephadex A-50 column system. The results indicate that the Sepharose column yields MM, MB, and BB isoenzymes uniquely, without cross contamination. Coefficients of variation (CV’s) for 10 replicate column assays were 2.8, 5.9, and 15.2% for 569 U of MM per liter, 82.3 U of MB per liter, and 9.0 U of BB per liter, respectively. The serum sample was enriched with baboon heart extract. Day-to-day reproducibility for a serum control assayed on 10 days yielded CV’s of 4.6, 9.9, and 40.3% for 391, 45.3 and 1.9 U of isoenzymes MM, MB, and BB per liter, respectively. A reference interval for each isoenzymes was derived from data on 81 men and 63 women.

Effect of serum pH on storage stability and reaction lag phase of human creatine kinase isoenzymes.

1980 ◽  
Vol 26 (8) ◽  
pp. 1165-1169 ◽  
Author(s):  
D A Nealon ◽  
S M Pettit ◽  
A R Henderson
Keyword(s):  
Creatine Kinase ◽  
Ethylene Glycol ◽  
Storage Stability ◽  
Kinase Assay ◽  
Lag Phase ◽  
Creatine Kinase Isoenzyme ◽  
Sh Groups ◽  
C Storage ◽  
Creatine Kinase Isoenzymes

Abstract We report the effect of serum pH on the storage stability of the human creatine kinase isoenzymes and on the creatine kinase assay lag phase (Szasz et al., Clin. Chem. 22: 650, 1976). We also investigated the effect of including mercaptoethanol, N-acetyl-L-cysteine, monothioglycerol, ethylenediaminetetraacetate, or ethylene glycol bis(betaaminoethyl ether)-N,N,N',N'-tetraacetate at 20, 4, and --20 degrees C. Storage stability of the isoenzymes is profoundly affected by pH. For patients' samples and semi-purified human creatine kinase isoenzymes added to heat-inactivated sera, increasing diluent pH above 7.0 decreases creatine kinase stability. The thiol agents or chelators generally give little or no protection above pH 7.5; at pH 8.5 they contribute significantly to isoenzyme instability. Storage at 4 degrees C provides greater stability than storage at 20 degrees C, particularly in the case of creatine kinase isoenzyme BB. The lag phase was minimum at a serum pH of 6.5, in the presence of 10 mmol of monothioglycerol per liter. Increasing serum pH to 8.5 prolongs the reaction lag phase by about 1 min over the minimum. We recommend that, before they are stored at 4 degrees C, the pH of patients' samples be adjusted to 6.5 and oxidation of SH-groups be minimized by adding monothioglycerol to the sample.

Isoenzymes of creatine kinase in extracts of various parts and regions of the human central nervous system.

1980 ◽  
Vol 26 (6) ◽  
pp. 760-762 ◽  
Author(s):  
R R Petronia ◽  
A H Maas ◽  
C W van Veelen ◽  
G E Staal
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Creatine Kinase ◽  
Gel Electrophoresis ◽  
Cauda Equina ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Human Central Nervous System ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Isoenzymes

Abstract The distribution of isoenzymes of creatine kinase (EC 2.7.3.2.) was investigated by agarose gel electrophoresis of extracts of selected parts and regions of the human central nervous system. Besides the major brain isoenzyme BB, we demonstrated the presence of three other creatine kinase isoenzyme forms. The distribution of creatine kinase isoenzymes depending strongly on the region from which the biopsy was taken. We found substantial amounts of the MB isoenzyme in extracts of the dura from the cauda equina of the two adults examined.

Creatine kinase isoenzyme patterns in human tissue obtained at surgery.

1976 ◽  
Vol 22 (2) ◽  
pp. 173-175 ◽  
Author(s):  
S H Tsung
Keyword(s):  
Creatine Kinase ◽  
Human Tissue ◽  
Creatine Kinase Isoenzyme ◽  
Quantitative Distribution ◽  
Immunological Method ◽  
Creatine Kinase Isoenzymes ◽  
Isoenzyme Patterns ◽  
Postmortem Autolysis

Abstract Chromatography on DEAE-Sephadex A-50 was applied to study the quantitative distribution of creatine kinase isoenzymes in extracts of human tissue obtained during surgery. The results are compared with those determined by an immunological method [Clin. Chim. Acta 58, 223 (1975)]. Conflicting results for some organs as reported by the two methods are probably attributable to postmortem autolysis.

heterogeneity of creatine kinase isoenzyme MM in serum in myocardial infarction: interconversion of the "normal" and "abnormal" sub-bands by glutathione

1990 ◽  
Vol 36 (5) ◽  
pp. 775-777 ◽  
Author(s):  
J Williams ◽  
K M Williams ◽  
T Marshall
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Creatine Kinase ◽  
Reduced Glutathione ◽  
Serum Creatine Kinase ◽  
Final Concentration ◽  
Oxidized Glutathione ◽  
Creatine Kinase Isoenzyme ◽  
Sequence Of Events ◽  
Opposite Sequence

Abstract We used isoelectric focusing (IEF) in polyacrylamide gels to investigate the effects of glutathione on the sub-bands of serum creatine kinase (CK; EC 2.7.3.2) isoenzyme MM in acute myocardial infarction. The intensity of the "abnormal" sub-bands c (pI 7.25), e (pI 6.85), and g (pI 6.50) increased, and that of the "normal" sub-bands 1 (pI 6.91), 2 (pI 6.65), and 3 (pI 6.35) decreased, following serum incubation with reduced glutathione (GSH, final concentration 1.25 mmol/L). Further incubation with oxidized glutathione (GSSG, final concentration 5 mmol/L) reversed this change and restored the original pattern, whereas GSSG at 7.5 mmol/L caused sub-bands c, e, and g to disappear and sub-bands 1, 2, and 3 to be enhanced. Sequential incubation of serum with 2.5 mmol of GSSG and 7.5 mmol of GSH per liter produced the opposite sequence of events; i.e., the "abnormal" sub-bands disappeared then reappeared (and GSH at 10 mmol/L enhanced their reappearance). At higher concentrations, glutathione (GSH or GSSG) impaired the detection of the CK-MM sub-bands after IEF, an effect that was "quenched" by heat-inactivated serum of low CK activity. Likewise, the intensity of tissue CK-MM (corresponding to myocardium extracted into 100 mmol/L Tris HCl buffer, pH 7.4) was greatly enhanced by adding heat-inactivated serum to the tissue extract before IEF. We discuss the significance of these findings for the diagnosis of myocardial infarction.

Creatine kinase isoenzyme activity in human placenta and in serum of women in labor.

1977 ◽  
Vol 23 (7) ◽  
pp. 1329-1332 ◽  
Author(s):  
H M Laboda ◽  
V J Britton
Keyword(s):  
Creatine Kinase ◽  
Human Placenta ◽  
Geometric Mean ◽  
Arithmetic Mean ◽  
Premature Labor ◽  
Induced Labor ◽  
Creatine Kinase Isoenzyme ◽  
Diethylaminoethyl Cellulose ◽  
Wet Weight ◽  
Cesarian Section

Abstract Creatine kinase (EC 2.7.3.2) isoenzymes in extracts of human placenta and in serum from nonpregnant women and women in labor were separated on columns containing diethylaminoethyl-cellulose and assayed. The distribution of the isoenzymes in placenta (n = 10) was 80% BB (200 +/- 66 U/g (wet weight), 19% MM (49 +/- 30 U/g), and 1% MB (2.6 +/- 1.7 U/g); The geometric mean for the serum BB activity of the nonpregnant women (n = 50) was 0.6 +/- 1.5 U/liter, as compared to 3.0 +/- 1.4 U/liter for patients in labor who had normal deliveries (n = 92). The arithmetic mean for serum BB activity of labor patients with induced labor (n = 20), premature labor (n = 7), cesarian section (n = 6), or hypertension and pre-eclampsia (n = 6) did not differ significantly from the arithmetic mean BB activity for serum of labor patients with normal deliveries. However, the arithmetic mean serum BB activity of patients with stillbirths (n = 7) was significantly smaller than the arithmetic mean for normal labor patients.

Serum creatine kinase isoenzyme BB as an indicator of active metastatic disease.

1979 ◽  
Vol 25 (6) ◽  
pp. 1190-1191 ◽  
Author(s):  
M H Zweig ◽  
L M Silverman ◽  
G B Dermer ◽  
A C Van Steirteghen
Keyword(s):  
Creatine Kinase ◽  
Metastatic Disease ◽  
Serum Creatine Kinase ◽  
Creatine Kinase Isoenzyme
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