Creatine kinase isoenzyme patterns in human tissue obtained at surgery.

1976 ◽  
Vol 22 (2) ◽  
pp. 173-175 ◽  
Author(s):  
S H Tsung

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.

1980 ◽  
Vol 26 (8) ◽  
pp. 1165-1169 ◽  
Author(s):  
D A Nealon ◽  
S M Pettit ◽  
A R Henderson

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.


1980 ◽  
Vol 26 (6) ◽  
pp. 760-762 ◽  
Author(s):  
R R Petronia ◽  
A H Maas ◽  
C W van Veelen ◽  
G E Staal

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.


2008 ◽  
Vol 14 (5) ◽  
pp. 257-260 ◽  
Author(s):  
H. W. Goedde ◽  
I. Christ ◽  
H. G. Benkmann ◽  
R. Beckmann ◽  
H. Lang

1980 ◽  
Vol 26 (13) ◽  
pp. 1888-1889 ◽  
Author(s):  
J Balaton ◽  
G N Hoag ◽  
C R Franks ◽  
C R Smith ◽  
W E DeCoteau

Abstract Normal peripheral nerve and neoplastic lesions of peripheral nerve varied in their creatine kinase (CK; EC 2.7.3.2) isoenzyme pattern, as assessed both with electrophoresis and with column chromatography. All three isoenzymes were seen in normal peripheral nerve, but the peripheral nerve tumors, neurofibroma and neurilemmoma, demonstrated predominantly CK-1 isoenzyme activity, with a trace amount of CK-3. No CK-2 activity was demonstrated in these tumors. In contrast, malignant schwannoma tissue contained all three isoenzymes, but in a different proportion than in normal peripheral nerve.


1980 ◽  
Vol 13 (4) ◽  
pp. 149-150 ◽  
Author(s):  
G.N. Hoag ◽  
C.R. Franks ◽  
C. Smith ◽  
W.E. DeCoteau

1983 ◽  
Vol 29 (8) ◽  
pp. 1537-1539 ◽  
Author(s):  
J P Steghens ◽  
I Maire ◽  
M Mathieu

Abstract We demonstrate that human placenta is a convenient source of creatine kinase isoenzyme BB. We compare the physicochemical and catalytic properties with those of other creatine kinase isoenzymes: purified human abdominal muscle MM and brain BB. We also describe a stabilizing medium for creatine kinase BB. Human placental and brain BB have similar catalytic properties, the respective Km values for creatine phosphate being 0.66 and 0.56 mmol/L and for adenosine diphosphate 89 and 70 nmol/L.


1980 ◽  
Vol 26 (6) ◽  
pp. 760-762 ◽  
Author(s):  
R R Petronia ◽  
A H Maas ◽  
C W van Veelen ◽  
G E Staal

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.


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