Creatine kinase isoenzymes: their separation and quantitation

Ogunro, Edward A.; Hearse, D. J.; Shillingford, John

doi:10.1093/cvr/11.2.94

Cited by 46 publications

(14 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It is known from the literature that in the heart muscle 30-41% of the total creatine kinase activity occurs äs MB isoenzyme in humans* 28 ± 2% in rats, 13 ± 4% in dogs and 4% in pigs (2,8,9,10). A rise in MB isoenzyme activity in the serum has been reported in rats after isoproterenöl-indüced cardiac damage (1), in dogs after occlusion of the left anterior descending coronary artery (9) and in rabbits in blood samples obtained after cardiac puncture (4).…”

Section: Resultsmentioning

confidence: 99%

Serum Isoenzyme Pattern of Creatine Kinase and Lactate Dehydrogenase in Various Animal Species

Preus¹,

Karsten²,

Bhargava³

1989

Clinical Chemistry and Laboratory Medicine

View full text Add to dashboard Cite

Summary:The creatine kinase and lactate^dehydrogenase isoenzyme pattera were determined in the serum of normal and untreated rats, rabbits, dogs, monkeys and pigs. The relative distribution of all isoenzymes in the serum and an electrophoretic pattern for each animal species are presented. The isoenzyme serum pattern showed a great Variation between the species. The diagnostic value of serum creatine kinase isoenzyme MB and lactate dehydrogenase isoenzymes l and 2 in predicting cardiac lesions in different animal species is briefly discussed.

show abstract

Section: Resultsmentioning

confidence: 99%

Serum Isoenzyme Pattern of Creatine Kinase and Lactate Dehydrogenase in Various Animal Species

Preus¹,

Karsten²,

Bhargava³

1989

Clinical Chemistry and Laboratory Medicine

View full text Add to dashboard Cite

show abstract

“…But, as Schon and co-workers (Shanske et al, 1987;Sakoda et al, 1988) have indicated, a lack of detection of M-PGM transcript does not exclude low transcription of M-PGM message in the brain. Most authors have reported that BB-CK is the only CK cytosolic isoenzyme present in human brain based upon electrophoretic (Deul and Van Breemen, 1964;Sjovall and Voigt, 1964;Dawson and Fine, 1967;Kumudavalli and Watts, 1968;Allard and Cabrol, 1970;Smith, 1972;Klein et al, 1973;Ogunro et al, 1977;Petronia et al, 1980;Urdal et al, 1983;Chandler et al, 1984;Chastain et al, 1988), chromatographic (Roberts et al, 1975;Tsung, 1976) and immunological techniques (Jockers-Wretou and Pfleiderer, 1975;Wevers et al, 1981;Chandler et al, 1984;Chastain et al, 1988). However, some authors have reported the presence of MM-CK.…”

Section: Discussionmentioning

confidence: 99%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumours

Durany

Joseph²,

Cruz-Sánchez³

et al. 1997

Br J Cancer

View full text Add to dashboard Cite

Summary The distribution of phosphoglycerate mutase (EC 5.4.2.1, PGM), 2,3-bisphosphoglycerate phosphatase (EC 3.1.3.13, BPGP) and creatine kinase (EC 2.7.3.2, CK) activity and isoenzymes in various regions of adult human brain and in brain tumours (astrocytomas, anaplastic astrocytomas, glioblastomas and meningiomas) has been determined using electrophoresis. PGM and cytosolic CK exist in mammalian tissues as three isoenzymes that result from the homodimeric and heterodimeric combinations of two subunits [types M (muscle) and B (brain)] coded by separated genes. In addition, a dimeric from and an octameric form of mitochondrial CK exist in mammals. Type BB-PGM was the major PGM isoenzyme found in normal brain, although type MB-PGM and type MM-PGM were also detected. All brain tumours possessed lower PGM activity than normal brain, and meningiomas showed higher BPGP activity. In astrocytic tumours, the proportion of type MB-and type MM-PGM decreased, and in meningiomas these isoenzymes were not detected. Type BB-CK and mitochondrial CK were the only CK isoenzymes detected in normal brain. Astrocytomas possessed lower CK activity than anaplastic astrocytomas and glioblastomas and, in addition, tended to possess lower CK content than normal brain. No qualitative changes of the normal CK isoenzyme pattern were observed in the tumours.Keywords: 2,3-bisphosphoglycerate phosphatase; creatine kinase; phosphoglycerate mutase; activity and isoenzymes; human brain; brain tumour Most isoenzyme transitions that occur in neoplastic tissues represent a shift from a differentiated to an undifferentiated pattern. The transitions to a more differentiated pattern are much less frequent and involve a great alteration in the control of gene expression. Omenn and co-workers (Omenn and Cheung, 1974;Omenn and Hermodson, 1975) described in human brain tumours a transition in the phosphoglycerate mutase phenotype from the normal brain pattern to a more differentiated muscle-type pattern that correlated with the degree of malignancy of the tumours and that could constitute a good brain tumour marker. As the series of tumours studied by Omenn and Cheung (1974) and Omenn and Hermodson (1975) was small and the distribution of phosphoglycerate mutase isoenzymes in human brain was poorly known, the present study was undertaken. In addition to phosphoglycerate mutase, we have determined creatine kinase, which possesses isoenzymes with a tissue distribution similar to those of phosphoglycerate mutase.Phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1, PGM) is a glycolytic enzyme present in mammalian cells in substantial amounts that catalyses the interconversion of 3-phosphoglycerate and 2-phosphoglycerate in the presence of the cofactor 2,3-bisphosphoglycerate. In addition to the mutase activity, it possesses 2,3-bisphosphoglycerate phosphatase Fothergill-Gilmore and Watson, 1989). Creatine kinase (ATP: creatine N-phosphotransferase, EC 2.7.3.2, CK) is an ubiquitous enzyme that functions in the transfer of energy from t...

show abstract

“…Samples with activity more than 250 mU/ml were diluted before determination of total CK; in order to minimise the dilutionactivation effect observed with plasma CK, heat inactivated plasma was used as the diluent (Graig et al, 1967). Isoenzymes were separated by electrophoresis on agarose gel and quantified in aqueous solution by fluorimetry (Ogunro et al, 1977). MB CK isoenzyme release curves were constructed by measuring the plasma MB CK activity (mU/ml) at the stated time intervals after the onset of chest pain.…”

Section: Methodsmentioning

confidence: 99%

Natural history and evaluation of ST segment changes and MB CK release in acute myocardial infarction.

Selwyn¹,

Ogunro²,

Shillingford³

1977

Heart

View full text Add to dashboard Cite

The experimental evidence relating ST segment elevation in the electrocardiogram to the progress and extent of ischaemic myocardial damage is discussed. There are difficulties in applying this to patients: the reproducibility of praecordial mapping was tested using a multiple analysis of variance. This showed that factors such as time after the onset of myocardial infarction and posture can affect measurements of sigmaST elevation significantly. There was a pattern of changes in segmaST elevation and of changes in plasma MB CK activity in a group of patients with uncomplicated anterior infarction. A significant byt weak correlation was found between sigmaST elevation in the first hour and the total MB CK activity released into the plasma, but not at any other time. The use of sigmaST elevation as a measure of the extent of ischaemic damage is unreliable. In 5 patients with a variety of complications of acute anterior infarction, changes in sigmaST elevation werr significantly different from the uncomplicated group, and MB CK release profiles suggested further necrosis. The pattern and time course of ST segment changes may be of use in assessing the progress of ischaemic myocardial damage.

show abstract

Creatine kinase isoenzymes: their separation and quantitation

Cited by 46 publications

References 0 publications

Serum Isoenzyme Pattern of Creatine Kinase and Lactate Dehydrogenase in Various Animal Species

Serum Isoenzyme Pattern of Creatine Kinase and Lactate Dehydrogenase in Various Animal Species

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumours

Natural history and evaluation of ST segment changes and MB CK release in acute myocardial infarction.

Contact Info

Product

Resources

About