Creatine kinase isoenzyme of high relative molecular mass in serum of a cancer patient.

1978 ◽  
Vol 24 (11) ◽  
pp. 2054-2057 ◽  
Author(s):  
H Yuu ◽  
Y Takagi ◽  
O Senju ◽  
J Hosoya ◽  
K Gomi ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Molecular Mass ◽  
Left Breast ◽  
Creatine Kinase Activity ◽  
Relative Molecular Mass ◽  
Anion Exchange Column ◽  
Creatine Kinase Isoenzyme ◽  
Heat Stable ◽  
Immunological Investigation ◽  
Therapeutic Radiation

Abstract We describe an atypical serum creatine kinase isoenzyme in the serum of a woman with cancer of the left breast. This isoenzyme migrated toward the cathode, closely following the MM isoenzyme on agarose gel electrophoresis. Its relative molecular mass was estimated to be about 325,000, fourfold that of normal creatine kinase. It is more heat-stable and is inhibited more by urea than the normal MM isoenzyme. Isoenzyme monomer B activity was observed to be 20 U/liter in the serum, as measured with use of an antibody against the M monomer. On anion-exchange column analysis, creatine kinase activity was observed only in the MM fraction, in spite of the fact that B activity was observed in the patient's serum. Results of the immunological investigation make it unlikely that the atypical isoenzyme is linked to immunoglobulin or beta-lipoprotein. It may have been present as the result of modification of normal creatine kinase by the therapeutic radiation the patient was receiving.

Interaction between human IgG and human creatine kinase isoenzyme-1 in serum: a route for the intravascular catabolism of creatine kinase-1?

1979 ◽  
Vol 25 (1) ◽  
pp. 112-116 ◽  
Author(s):  
V Prabhakaran ◽  
D A Nealon ◽  
A R Henderson
Keyword(s):  
Creatine Kinase ◽  
Immunoglobulin G ◽  
Kinase Activity ◽  
Chelating Agent ◽  
Creatine Kinase Activity ◽  
Relative Molecular Mass ◽  
Creatine Kinase Isoenzyme ◽  
Enzyme Degradation ◽  
Detectable Serum

Abstract In vitro incubation, at 37 degrees C, of human creatine kinase isoenzyme-1 (isoenzyme BB) and human immunoglobulin G in a buffer results in the formation of a complex of high relative molecular mass (Mr approximately 825,000), which contains both proteins. This complex also forms in vitro if creatine kinase isoenzyme-1 is incubated with fresh human serum. The creatine kinase activity of the complex obtained from either incubation is extremely labile, even in the presence of a chelating agent and a thioglycerol. We present evidence for the existence of this complex in the sera of patients who have detectable serum creatine kinase isoenzyme-1 activity. Sera with high activities of creatine kinase isoenzyme-2 do not appear to have this complex. We therefore speculate that complexing of creatine kinase isoenzyme-1 with serum immunoglobulin G may be a pathway of enzyme degradation.

Ratio of Creatine Kinase 2 Mass Concentration to Total Creatine Kinase Activity not Altered by Heavy Physical Exercise

1992 ◽  
Vol 38 (11) ◽  
pp. 2224-2227 ◽  
Author(s):  
J Ordóñez-Llanos ◽  
J R Serra-Grima ◽  
J Mercé-Muntañola ◽  
F González-Sastre
Keyword(s):  
Creatine Kinase ◽  
Mass Concentration ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Marathon Runners ◽  
Creatine Kinase Isoenzyme ◽  
Total Creatine Kinase Activity ◽  
Total Creatine ◽  
Sedentary Subjects

Abstract Serum creatine kinase isoenzyme 2 concentrations (CK 2 mass) were measured in marathon runners during training and 1 and 2 days after a race and compared with values from 36 acute myocardial infarction (AMI) patients whose total CK and (or) CK 2 activities were similar to those of runners in the basal state. During training, runners had CK and CK 2 activities 53% and 43% above reference values, respectively, and 36% had CK 2 activity > 5% of total CK. Nine runners (26%) showed CK 2 mass values > 6 micrograms/L but < or = 10 micrograms/L; 35 of the AMI subjects, despite having CK activities similar to those of runners, had values > 10 micrograms/L. The ratio of CK 2 mass to total CK activity was significantly (P < 0.0002) different between sexes for runners. At 1 and 2 days after racing, 100% of CK and CK 2 activities and 71% and 57% of the percentages of CK 2 activity, respectively, were abnormally high; 57% and 43% of CK 2 mass values were > 10 micrograms/L, being comparable with those observed for the AMI group. Basal CK 2 mass values of the runners appeared only slightly higher than that for sedentary subjects, but after exercise half the subjects presented increased values similar to those observed for AMI subjects. The ratio of CK 2 mass to total CK activity appeared unaltered by exercise in all but one of the samples assayed, indicating its utility in evaluating CK 2 mass increases originating in skeletal muscle.

Creatine kinase:aspartate aminotransferase activity ratio as an indicator of the source of an increased creatine kinase activity.

1988 ◽  
Vol 34 (12) ◽  
pp. 2506-2510 ◽  
Author(s):  
D R Dufour
Keyword(s):  
Myocardial Infarction ◽  
Skeletal Muscle ◽  
Acute Myocardial Infarction ◽  
Creatine Kinase ◽  
Retrospective Study ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Creatine Kinase Activity ◽  
Aminotransferase Activity ◽  
Creatine Kinase Isoenzyme

Abstract Although measurements of creatine kinase isoenzyme 2 (CK-MB) are often used to diagnose acute myocardial infarction, their sensitivity and specificity are less than 100%. Because skeletal muscle contains more CK and less aspartate aminotransferase (AST) than cardiac muscle, the CK/AST ratio might provide a useful adjunct in evaluating the source of a supranormal value for CK. I established the following decision levels in a retrospective study of 342 patients: ratios less than 14 (if total CK was 300-1200 U/L), less than 20 (CK 1201-2000 U/L), or less than 25 (CK greater than 2000 U/L) suggested myocardial infarction, with a sensitivity of 95% and a specificity of 65%. In a validation study with 277 additional patients, liver disease and alcohol abuse caused erroneous results, leading to exclusion of 22% of these patients. In the remaining cases, sensitivity was 94%, specificity 90%. The CK/AST ratios changed little with time, suggesting that a single value would be adequate for evaluating patients with increased CK.

Crystalline mitochondrial inclusion bodies isolated from creatine depleted rat soleus muscle

1997 ◽  
Vol 110 (12) ◽  
pp. 1403-1411
Author(s):  
E. O'Gorman ◽  
K.H. Fuchs ◽  
P. Tittmann ◽  
H. Gross ◽  
T. Wallimann
Keyword(s):  
Creatine Kinase ◽  
Molecular Mass ◽  
Inclusion Bodies ◽  
Gel Filtration ◽  
Three Dimensional ◽  
Creatine Kinase Activity ◽  
Mitochondrial Creatine Kinase ◽  
Two Dimensional Image ◽  
Acid Diet ◽  
Creatine Uptake

Rats were fed a 2% guanidino propionic acid diet for up to 18 weeks to induce cellular creatine depletion by inhibition of creatine uptake by this creatine analogue. Ultrastructural analysis of creatine depleted tissues showed that mitochondrial intermembrane inclusion bodies appeared in all skeletal muscles analysed, after 11 weeks of feeding. Heart had relatively few even after 18 weeks of analogue feeding and none were evident in kidney, brain or liver. These structures were strongly immuno-positive for sarcomeric mitochondrial creatine kinase and upon removal from mitochondria, the inclusion bodies were shown to diffract to a resolution of 2.5 nm. Two-dimensional image analysis and three-dimensional reconstruction revealed arrays of creatine kinase octamers with additional components between the octameric structures. The same mitochondria had a 3-fold higher extractable specific creatine kinase activity than controls. Molecular mass gel filtration of inclusion body containing mitochondrial extracts from analogue fed rat solei revealed mitochondrial creatine kinase eluting as an aggregate of an apparent molecular mass > or = 2,000 kDa. Mitochondrial creatine kinase of control soleus mitochondrial extract eluted as an octamer, with a molecular mass of 340 kDa. Respiration measurements of control solei mitochondria displayed creatine mediated stimulation of oxidative phosphorylation that was absent in analogue-fed rat solei mitochondria. The latter also had 19% and 14% slower rates of state 4 and maximal state 3 respiration, respectively, than control mitochondria. These results indicate that mitochondrial creatine kinase co-crystallises with another component within the inter membrane space of select mitochondria in creatine depleted skeletal muscle, and is inactive in situ.

A high molecular mass phosphoprotein defined by a novel monoclonal antibody is closely associated with the intermicrotubule cross bridges in the Trypanosoma brucei cytoskeleton

1992 ◽  
Vol 103 (3) ◽  
pp. 665-675 ◽  
Author(s):  
A. Woods ◽  
A.J. Baines ◽  
K. Gull
Keyword(s):  
Molecular Mass ◽  
Trypanosoma Brucei ◽  
Minor Component ◽  
Relative Molecular Mass ◽  
Microtubule Associated Proteins ◽  
Heat Stable ◽  
Cytoplasmic Face ◽  
Associated Proteins ◽  
Cross Bridges ◽  
Main Component

The main component of the cell body cytoskeleton of Trypanosoma brucei is the highly organised array of stable, subpellicular microtubules on the cytoplasmic face of the plasma membrane. Although several microtubule associated proteins (MAPs) have been shown to be associated with this array, the mechanisms by which individual microtubules interact with one another and with the membrane are still largely undetermined. In this study we have used the T. brucei cytoskeleton as a complex immunogen for the production of monoclonal antibodies to define novel cytoskeletal antigens. Screening by immunofluorescence enabled the selection of an antibody, WCB-1, which detects an antigen associated specifically with the subpellicular microtubules and not with the flagellum microtubules. The antigen (WCB210) was shown to have a relative molecular mass of 210,000 by western blotting. Immunogold studies showed the epitope to be located on the membrane-facing side of the subpellicular cage; it appears to be closely associated with the cross-bridges lying between the microtubules. Unlike many MAPs this protein was shown not to be heat stable and is predicted to be a roughly globular monomer. Even though WCB210 is a very minor component of the cytoskeleton it is heavily phosphorylated. It is possible that this protein is involved in regulation of the subpellicular microtubule crossbridges by interaction with other proteins.

Detection of Cardiac-Specific Creatine Kinase Isoenzyme in Sera with Normal or Slightly Increased Total Creatine Kinase Activity

1975 ◽  
Vol 21 (8) ◽  
pp. 1088-1092 ◽  
Author(s):  
Donald W Mercer ◽  
Murray A Varat
Keyword(s):  
Creatine Kinase ◽  
Time Course ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Good Reproducibility ◽  
Kinetic Assay ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Mb ◽  
Total Creatine Kinase Activity ◽  
Total Creatine

Abstract We describe a spectrophotometric kinetic assay for detecting creatine kinase MB isoenzyme activity in the 1 to 10 U/liter range. The MB isoenzyme was isolated [Clin. Chem. 20, 36 (1974)] and assayed (Rosalki method) with an Abbott ABA-100. Good reproducibility was demonstrated for MB isoenzyme activities near 1 U/liter (CV = 2.6%). Sera with normal or slightly increased total creatine kinase activity were evaluated. Sera of 14 patients with acute myocardial infarction contained, per liter, 84 to 236 U of total creatine kinase activity and 4.6 to 28.0 U of isoenzyme MB activity; corresponding ranges for sera from healthy lab technicians and patients with noncardiac disease were 36 to 277 and 0 to 2.6 U. MB isoenzyme activity for infarction patients rose and fell sharply within three days after the infarction. Atypical time-course patterns, MB isoenzyme activity remaining abnormally great for five days, were observed in serum from patients with prolonged atrial fibrillation and congestive heart failure or cardiomyopathy; the BB isoenzyme (1 to 5 U/liter) was also detected in sera of such patients but was absent in sera from infarction patients. Quantification of column-isolated MB by the assay described is rapid, easy, specific, and extremely sensitive for measuring MB in the 1 to 10 U/liter range.

Creatine kinase isoenzyme variants in human serum.

1978 ◽  
Vol 24 (5) ◽  
pp. 832-834 ◽  
Author(s):  
L Ljungdahl ◽  
W Gerhardt
Keyword(s):  
Experimental Data ◽  
Creatine Kinase ◽  
Kinase Activity ◽  
Normal Values ◽  
Creatine Kinase Activity ◽  
Inhibitory Antibody ◽  
Creatine Kinase Isoenzyme ◽  
Total Creatine Kinase Activity ◽  
Total Creatine ◽  
Subunit B

Abstract In serum from about 800 patients, total creatine kinase and its subunit B activities were determined by the recommended Scandinavian creatine kinase method in the absence and presence of a creatine kinase M subunit inhibitory antibody. Eight patients had supranormal subunit B activities, but normal or near-normal values for total creatine kinase activity. Electrophoresis of sera from these eight patients showed, in addition to the normally migrating isoenzyme MM, one or two abnormally migrating creatine kinase isoenzyme bands, located between normally migrating isoenzymes MM and MB. Experimental data suggest that these abnormal bands may be isoenzyme BB with changed electrophoretic mobility. The eight patients had no particular disorder in common.

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