Human placenta as a convenient source of creatine kinase BB.

1983 ◽  
Vol 29 (8) ◽  
pp. 1537-1539 ◽  
Author(s):  
J P Steghens ◽  
I Maire ◽  
M Mathieu
Keyword(s):  
Creatine Kinase ◽  
Human Placenta ◽  
Catalytic Properties ◽  
Adenosine Diphosphate ◽  
Creatine Phosphate ◽  
Abdominal Muscle ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Bb ◽  
Creatine Kinase Isoenzymes

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.

Effect of serum pH on storage stability and reaction lag phase of human creatine kinase isoenzymes.

1980 ◽  
Vol 26 (8) ◽  
pp. 1165-1169 ◽  
Author(s):  
D A Nealon ◽  
S M Pettit ◽  
A R Henderson
Keyword(s):  
Creatine Kinase ◽  
Ethylene Glycol ◽  
Storage Stability ◽  
Kinase Assay ◽  
Lag Phase ◽  
Creatine Kinase Isoenzyme ◽  
Sh Groups ◽  
C Storage ◽  
Creatine Kinase Isoenzymes

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.

Isoenzymes of creatine kinase in extracts of various parts and regions of the human central nervous system.

1980 ◽  
Vol 26 (6) ◽  
pp. 760-762 ◽  
Author(s):  
R R Petronia ◽  
A H Maas ◽  
C W van Veelen ◽  
G E Staal
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Creatine Kinase ◽  
Gel Electrophoresis ◽  
Cauda Equina ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Human Central Nervous System ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Isoenzymes

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.

Creatine kinase isoenzyme patterns in human tissue obtained at surgery.

1976 ◽  
Vol 22 (2) ◽  
pp. 173-175 ◽  
Author(s):  
S H Tsung
Keyword(s):  
Creatine Kinase ◽  
Human Tissue ◽  
Creatine Kinase Isoenzyme ◽  
Quantitative Distribution ◽  
Immunological Method ◽  
Creatine Kinase Isoenzymes ◽  
Isoenzyme Patterns ◽  
Postmortem Autolysis

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.

Creatine kinase isoenzyme activity in human placenta and in serum of women in labor.

1977 ◽  
Vol 23 (7) ◽  
pp. 1329-1332 ◽  
Author(s):  
H M Laboda ◽  
V J Britton
Keyword(s):  
Creatine Kinase ◽  
Human Placenta ◽  
Geometric Mean ◽  
Arithmetic Mean ◽  
Premature Labor ◽  
Induced Labor ◽  
Creatine Kinase Isoenzyme ◽  
Diethylaminoethyl Cellulose ◽  
Wet Weight ◽  
Cesarian Section

Abstract Creatine kinase (EC 2.7.3.2) isoenzymes in extracts of human placenta and in serum from nonpregnant women and women in labor were separated on columns containing diethylaminoethyl-cellulose and assayed. The distribution of the isoenzymes in placenta (n = 10) was 80% BB (200 +/- 66 U/g (wet weight), 19% MM (49 +/- 30 U/g), and 1% MB (2.6 +/- 1.7 U/g); The geometric mean for the serum BB activity of the nonpregnant women (n = 50) was 0.6 +/- 1.5 U/liter, as compared to 3.0 +/- 1.4 U/liter for patients in labor who had normal deliveries (n = 92). The arithmetic mean for serum BB activity of labor patients with induced labor (n = 20), premature labor (n = 7), cesarian section (n = 6), or hypertension and pre-eclampsia (n = 6) did not differ significantly from the arithmetic mean BB activity for serum of labor patients with normal deliveries. However, the arithmetic mean serum BB activity of patients with stillbirths (n = 7) was significantly smaller than the arithmetic mean for normal labor patients.

Stability and electrophoretic characteristics of creatine kinase BB extracted from human brain and intestine.

1988 ◽  
Vol 34 (3) ◽  
pp. 489-492 ◽  
Author(s):  
S L Chastain ◽  
C H Ketchum ◽  
W E Grizzle
Keyword(s):  
Myocardial Infarction ◽  
Creatine Kinase ◽  
Human Brain ◽  
False Positive ◽  
Human Intestine ◽  
Electrophoretic Variant ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Bb ◽  
Similar Development ◽  
Creatine Kinase Isoenzyme Mb

Abstract Creatine kinase (CK; EC 2.7.3.2) isoenzyme BB extracted from brains of rats reportedly undergoes modification at 37 degrees C, leaving an electrophoretic variant that accounts for most of the residual CK activity. This variant, called CK-BB', migrates on electrophoresis similarly to creatine kinase isoenzyme MB. Using electrophoresis and immunoinhibition with antiserum to creatine kinase isoenzyme MM, we found CK-BB to be the only identifiable cytoplasmic isoenzyme in surgical samples from human brain and intestine. In contrast, we found that some samples of brain obtained at autopsy contain CK-BB'. We also found that CK-BB extracted from human brain was converted to CK-BB' upon incubation in serum or plasma at 37 degrees C. We found a similar development of CK-BB' in incubation mixtures of serum or plasma containing CK-BB obtained from surgical samples of human intestine. The development of CK-BB' during infarction of the gastrointestinal system may thus be a source of false-positive CK-MB in the laboratory verification of myocardial infarction when electrophoresis is used as the only method to identify CK isoenzymes.

Regulation of Creatine Kinase Isoenzymes in Human Placenta During Early, Mid-, and Late Gestation

1996 ◽  
Vol 3 (6) ◽  
pp. 322-327 ◽  
Author(s):  
Michael F. Thomure ◽  
Michael J. Gast ◽  
Neelam Srivastava ◽  
R. Mark Payne
Keyword(s):  
Creatine Kinase ◽  
Human Placenta ◽  
Late Gestation ◽  
Creatine Kinase Isoenzymes

Effect of macro creatine kinase BB on results of different creatine kinase isoenzyme methods.

1982 ◽  
Vol 28 (6) ◽  
pp. 1400-1400 ◽  
Author(s):  
M R Pudek ◽  
B E Jacobson ◽  
N Urquhart ◽  
S W Rabkin
Keyword(s):  
Creatine Kinase ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Bb

Creatine kinase response surfaces explored by use of factorial experiments and simplex maximization.

1983 ◽  
Vol 29 (5) ◽  
pp. 793-799 ◽  
Author(s):  
D M Fast ◽  
E J Sampson ◽  
V S Whitner ◽  
M Ali
Keyword(s):  
Creatine Kinase ◽  
Response Surface ◽  
Kinase Activity ◽  
Adenosine Diphosphate ◽  
Creatine Phosphate ◽  
Creatine Kinase Activity ◽  
Response Surfaces ◽  
Optimal Conditions ◽  
Reaction Conditions ◽  
Sensitivity Reaction

Abstract We conducted a five-component, five-level response-surface experiment to optimize the pH and the concentrations of magnesium, creatine phosphate, adenosine diphosphate, and buffer in an assay for creatine kinase. Under optimal conditions, creatine kinase activity was about 5% greater than that obtained with a previously reported assay (Clin Chem 23: 1569, 1977). We also applied a simplex maximization algorithm to the response-surface equation to locate areas of maximum sensitivity. Reaction conditions for two such areas were found, each yielding approximately 11% more activity than with the previously reported method.

Transformation of creatine kinase-BB isoenzyme in vitro: effect of carboxylic acids, thiols, pH, cations, and chelators.

1982 ◽  
Vol 28 (12) ◽  
pp. 2414-2417 ◽  
Author(s):  
J A Lott ◽  
J W Heinz
Keyword(s):  
Creatine Kinase ◽  
Rat Brain ◽  
Carboxylic Acids ◽  
Alkaline Ph ◽  
Creatine Kinase Isoenzyme ◽  
Creatine Kinase Bb ◽  
Vitro Effect ◽  
Dialyzed Serum

Abstract Creatine kinase isoenzyme BB from rat brain was incubated with serum, dialyzed serum, or plasma, with added carboxylic acids, thiols, buffers, or cations. It was found to be very unstable at 37 degrees C under all these conditions, being transformed to CK-BB', a form that migrates like CK-MB on agarose electrophoretic plates. This transformation is enhanced at alkaline pH and, especially, by Zn2+. CK-BB' is quite stable, and probably results from binding of cations to CK-BB, because the transformation is prevented by EDTA and citrate.

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