Die Instabilit�t der Kreatin-Phosphokinase-Isoenzyme im Serum

Frotscher, Ulrich; Dominik, B.; Richter, R.; Zschaege, B; M, Schulte-Lippern; Jenett, G.; Messerschmidt, W.; Schmidtmann, W.; Wilbrandt, R

doi:10.1007/bf01468074

Cited by 14 publications

(6 citation statements)

References 26 publications

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“…Contrary to what might be ex pected, MM-CK, rather than BB isoenzyme, has been found elevated in the serum of patients with acute brain diseases (1,4,6,9,12). This paradoxical finding has no clear explanation as yet.…”

Section: Introductioncontrasting

confidence: 44%

Enzymic, Electrophoretic and Immunoreactive Properties of Labeled MM and BB Isoenzymes of Human Creatine Kinase

Fang

Cho

Meltzer

1978

Enzyme

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Purified MM and BB isoenzymes of human creatine kinase (CK) were labeled with Bolton-Hunter reagent. Labeling process did not affect their enzymic activity, although the labeled enzymes lost enzymic activity in storage. The labeled BB isoenzyme progressively changed its electrophoretic mobility, while labeled MM isoenzyme did not. Both labeled isoenzymes, however, maintained their immunoreactivity with their respective antisera. These results suggest that the enzymic and the immunoreactive sites of each CK isoenzyme are different and that BB isoenzyme, not MM isoenzyme, is electrophorectically unstable.

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Section: Introductioncontrasting

confidence: 44%

Enzymic, Electrophoretic and Immunoreactive Properties of Labeled MM and BB Isoenzymes of Human Creatine Kinase

Fang

Cho

Meltzer

1978

Enzyme

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“…Several studies have shown that CK is inactivated by human plasma and serum, [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24] and have shown that the three CK isoenzymes (MM, MB, and BB) are differently affected: MM CK is the most stable isoenzyme, MB CK is slightly less stable, and BB CK is the least stable isoenzyme. 9 15-18 20 21 The rate of CK inactivation increased with temperature.…”

Section: Discussionmentioning

confidence: 99%

“…It has been reported that in the plasma of these patients both CK and PGM activities increase, although the increase in PGM activity is not as striking as that seen for CK. 6 7 It is known that CK is also inactivated by plasma and serum, [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24] and uric acid is one serum component that has been shown to participate in this inactivation. 10 11 15 Our present study was undertaken to characterise the inactivation of PGM by serum and to ascertain whether or not urate is involved.…”

mentioning

confidence: 99%

Inactivation of phosphoglycerate mutase and creatine kinase isoenzymes in human serum

Durany

Carreras²,

Valenti³

et al. 2002

Molecular Pathology

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Aims/Background: Total phosphoglycerate mutase (PGM) activity in serum has been shown to be increased in acute myocardial infarction with the same time course as creatine kinase (CK) activity. However, the increase in the muscle (MM) and in the cardiac (MB) PGM isoenzymes was not as high as expected. The present study was undertaken to characterise PGM inactivation by serum and to compare it with serum CK inactivation. Methods: The PGM and the CK activities of extracts of human heart, skeletal muscle, and brain were determined spectrophotometrically after incubation with different media, namely: plasma, whole serum, dialysed serum, heated serum, serum ultrafiltrate, urate solution, and buffer solution. Results: Type MM PGM was inactivated by plasma, whole serum, heated serum, dialysed serum, and serum ultrafiltrate. Inactivation in dialysed serum was reduced by EDTA and largely reversed by thiol agents. Inactivation in serum ultrafiltrate was not prevented by EDTA and only partially reversed by dithiothreitol. The muscle and type BB CK isoenzymes were inactivated in all the tested media. The incubation of human and rabbit skeletal muscle PGM and CK in urate solution showed that urate does not affect mutase activity under conditions that inactivate CK. Conclusions: These results confirm the mechanisms of CK inactivation proposed by others and show that the type M PGM subunit is inactivated by two different mechanisms, which appear to involve the thiol groups of the enzyme. One mechanism is caused by either a protein component or a protein bound serum component and involves calcium ions and/or another chelatable metal ion. The other mechanism is caused by a lower molecular weight serum component and is metal ion independent.

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“…Enzyme inactivation is accompanied by parallel changes in the electrophoretic mobility of creatine kinase-BB (5,6,7). Enzyme inactivation is accompanied by parallel changes in the electrophoretic mobility of creatine kinase-BB (5,6,7).…”

Section: Contributionsmentioning

confidence: 99%

Workshop conference report

1983

CCLM

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It was the aim of the workshop to summarize present knowledge of the variant creatine kinases in human blood. Discussion was centered on the nature, measurement, and clinical significance pfthese variants. On the basis of the presented results, the different creatine kinase variants can be classified äs follows: Normal size variants (80000 Daltons)These originale from postsynthetic modifications of the three dimeric isoenzymes creatine kinase-MM, MB or BB. The M subunit can be transformed by a serum constituent and these modifications result in at least three different creatine kinase-MM and two creatine kinase-MB variants, which still show catälytic activity.The mechanism of the postsynthetic alterations of creatine kinase-BB seems to be more complex: In vitro incubation of this isoenzyme even in a non-serum matrix changes its electrophoretic rnobility and decreases activity. In vivo there is evidence that on the one hand intact creatine kinase-BB molecules are directly removed from the circulation. On the other hand, however, inactive creatine kinase-BB-protein is reported to occur in serum. Variants with higher molecular weights (> 200 000 Daltons)These are termed macro creatine kinases.Macro creatine kinase type l comprises the immunoglobulin-bound creatine kinase isoenzyirfcs. Of these immune complexes, IgG-linked creatine kinäse-BB is well known and has been described in detail, whereas the occurrence of creatine kinase-MM-containing macro creatine kinases is still questionable. Macro creatine kinase type l is found in the blood of about 2% of all hospitalized patients. It occurs mainly in elderly women, but it is not known whether it has any special clinical significance.

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Die Instabilit�t der Kreatin-Phosphokinase-Isoenzyme im Serum

Cited by 14 publications

References 26 publications

Enzymic, Electrophoretic and Immunoreactive Properties of Labeled MM and BB Isoenzymes of Human Creatine Kinase

Enzymic, Electrophoretic and Immunoreactive Properties of Labeled MM and BB Isoenzymes of Human Creatine Kinase

Inactivation of phosphoglycerate mutase and creatine kinase isoenzymes in human serum

Workshop conference report

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