An assay for creatine kinase conversion factor

Falter, H.; Michelutti, Lisa; Mazzuchin, A.; Whiston, W.

doi:10.1016/s0009-9120(82)90096-0

Cited by 8 publications

(2 citation statements)

References 29 publications

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“…Recently, a quantitative method has been described to estimate the amount of the CK-conversion factor in human serum [5,10]. That method is based on calculation of the decrease per unit of time of the percentage of unmodified M-chains.…”

Section: Resultsmentioning

confidence: 99%

Purification and determination of the modifying protein responsible for the post-synthetic modification of creatine kinase (EC 2.7.3.2) and enolase(EC 4.2.1.11)

Landeghem

Soons

Wever

et al. 1985

Clinica Chimica Acta

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SummaryThe purification of a serum protein, responsible for the postsynthetic modification of CK and enolase, is described. A purification of about 1300-fold could be reached after subsequent chromatography of human serum on DEAE cellulose and Sephacryl S-200 Superfine followed by affinity chromatography using antibodies against human serum albumin, C3 and C4 and against total human serum proteins. A recovery of 160% of modifying activity was found. The molecular mass and the isoelectric point of the modifying protein have been determined.It is concluded that the concentration of the modifying protein in human serum is < 210 mg/l.

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Section: Resultsmentioning

confidence: 99%

Purification and determination of the modifying protein responsible for the post-synthetic modification of creatine kinase (EC 2.7.3.2) and enolase(EC 4.2.1.11)

Landeghem

Soons

Wever

et al. 1985

Clinica Chimica Acta

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“…This 'converts' the single band of a skeletal-muscle extract, resolved by agarose-gel electrophoresis, into a triple-banded pattern. The slowest band corresponds to the original MM isoenzyme, and the intermediate and fastest forms are thought to represent modification of one and both subunits respectively (Wevers et al, 1978;Yasmineh et al, 1981;Falter et al, 1982;Edwards & Watts, 1983). Some enzyme activity is lost during conversion of the native MM isoenzyme in vitro; thiols stabilize the enzyme, but also inhibit CK-conversion-factor activity.…”

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Human ‘creatine kinase conversion factor’ identified as a carboxypeptidase

Edwards¹,

Watts²

1984

Biochemical Journal

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The effect of partially purified 'creatine kinase conversion factor' on rabbit muscle creatine kinase is shown to be that of a carboxypeptidase, removing the C-terminal lysine residue from both subunits. These changes fully explain the three-banded electrophoretic patterns of the partially and the fully modified rabbit and human enzymes. The factor also produces a similar electrophoretic pattern with haemoglobin A; comparison with the effects of carboxypeptidases A and B permits the inference that the C-terminal residues of both alpha- and beta-subunits are removed. Small synthetic peptides are poor or non-substrates. A low activity with hippuryl-L-lysine may be due to contamination of the preparation with carboxypeptidase N. The possibility has been excluded that the action of conversion factor on creatine kinase involves modification of the protein thiol groups. Mr, substrate-specificity, pH-activity profile and the effects of metal ions distinguish creatine kinase conversion factor from carboxypeptidases A, B and N. On the basis of this evidence it is proposed to give the conversion factor the provisional name of carboxypeptidase K.

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Tetrathionate-blocked creatine kinase as a substrate for human plasma ‘creatine kinase conversion factor’

Edwards

Watts

1983

Clinica Chimica Acta

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An assay for creatine kinase conversion factor

Cited by 8 publications

References 29 publications

Purification and determination of the modifying protein responsible for the post-synthetic modification of creatine kinase (EC 2.7.3.2) and enolase(EC 4.2.1.11)

Purification and determination of the modifying protein responsible for the post-synthetic modification of creatine kinase (EC 2.7.3.2) and enolase(EC 4.2.1.11)

Human ‘creatine kinase conversion factor’ identified as a carboxypeptidase

Tetrathionate-blocked creatine kinase as a substrate for human plasma ‘creatine kinase conversion factor’

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