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.

In vitro effect of elastase and cathepsin G from human neutrophils on creatine kinase and lactate dehydrogenase isoenzymes

1993 ◽  
Vol 39 (6) ◽  
pp. 986-992
Author(s):  
J A Stark ◽  
A R Henderson
Keyword(s):  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Hypochlorous Acid ◽  
Proteolytic Enzymes ◽  
Sodium Dodecyl ◽  
Cathepsin G ◽  
Human Neutrophils ◽  
Sample Treatment ◽  
Vitro Effect

Abstract The polymorphonuclear granulocyte, or neutrophil, has been implicated as a mediator of tissue-destructive events because it releases the preformed proteolytic enzymes elastase and cathepsin G, and, as a result of myeloperoxidase action, hypochlorous acid. We show that elastase inactivates and fragments creatine kinase isoenzymes CK-2 and CK-3, and, to a lesser extent, lactate dehydrogenase (LD) isoenzyme LD-1, whereas cathepsin G acts only on CK-2. Both neutrophil enzymes act on LD-3. The course of inactivation was followed by measuring the loss of catalytic activity at 37 degrees C. The evidence for fragmentation was obtained by gel filtration; electrophoresis after sample treatment with sodium dodecyl sulfate and 2-mercaptoethanol was less satisfactory for this purpose. Hypochlorous acid inactivates CK activity by about 75% at concentrations as low as 8 mumol/L and totally at concentrations > 140 mumol/L, whereas LD activity is not affected until concentrations exceed 200 mumol/L. After a myocardial infarction, the number of neutrophils increases; they are triggered and concentrate around damaged myocardial tissue. Our data suggest that neutrophils may inactivate and fragment "cardiac" enzymes released from such damaged tissue.

In Vitro Effect of Lead on Na+, K+-ATPase Activity in Different Regions of Adult Rat Brain

2003 ◽  
Vol 26 (2) ◽  
pp. 117-124 ◽  
Author(s):  
Prabhakara Rao Yallapragada ◽  
Jennifer Butler ◽  
Bokara Kiran Kumar ◽  
Bettaiya Rajanna
Keyword(s):  
Atpase Activity ◽  
Rat Brain ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Vitro Effect

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.

The in vitro effect of l-prolyl-l-leucyl-glycineamide (MIF-1) on the guanylate cyclase system of a crude rat brain mitochondrial fraction

Neuropeptides ◽  
1981 ◽  
Vol 1 (5) ◽  
pp. 391-400 ◽  
Author(s):  
A.R. Gerber ◽  
K.S. Wood ◽  
A.O. Sartor ◽  
W.F. Wheeler ◽  
T.C. Gayle ◽  
...  
Keyword(s):  
Rat Brain ◽  
Guanylate Cyclase ◽  
Mitochondrial Fraction ◽  
Vitro Effect

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.

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