Creatine Kinase: ATP Contaminating Creatine Phosphate Substrate of a Commercial Kit

1973 ◽  
Vol 19 (2) ◽  
pp. 280-281
Author(s):  
Joseph Tesfaye ◽  
Jacques Longpré ◽  
Frank Bodley
Keyword(s):  
Creatine Kinase ◽  
Creatine Phosphate ◽  
Commercial Kit

scholarly journals Molecular docking and density functional theory studies on creatine, guanidinoacetic acid, and their phosphorylated analogues binding to muscle creatine kinase

2020 ◽  
pp. 174751982097858
Author(s):  
M Vraneš ◽  
S Ostojić ◽  
Č Podlipnik ◽  
A Tot
Keyword(s):  
Density Functional Theory ◽  
Creatine Kinase ◽  
Molecular Docking ◽  
Density Functional ◽  
Creatine Phosphate ◽  
Docking Studies ◽  
Muscle Creatine Kinase ◽  
Functional Theory ◽  
Guanidinoacetic Acid ◽  
Muscle Creatine

Comparative molecular docking studies on creatine and guanidinoacetic acid, as well as their phosphorylated analogues, creatine phosphate, and phosphorylated guanidinoacetic acid, are investigated. Docking and density functional theory studies are carried out for muscle creatine kinase. The changes in the geometries of the ligands before and after binding to the enzyme are investigated to explain the better binding of guanidinoacetic acid and phosphorylated guanidinoacetic acid compared to creatine and creatine phosphate.

Single Stable Reagent for Creatine Kinase Assay

1971 ◽  
Vol 17 (6) ◽  
pp. 548-550 ◽  
Author(s):  
Charles Bishop ◽  
T M Chu ◽  
Z K Shihabi
Keyword(s):  
Creatine Kinase ◽  
Maximum Velocity ◽  
Creatine Phosphate ◽  
Spectrophotometric Assay ◽  
Kinase Assay ◽  
Reagent Cost ◽  
One Step ◽  
Stable Reagent

Abstract A single stable reagent for spectrophotometric assay of creatine kinase in one step is described. Reagent cost has been decreased by running the reaction at Km conditions for creatine phosphate and relating the activity to maximum velocity.

scholarly journals Creatine kinase expression and creatine phosphate accumulation are developmentally regulated during differentiation of mouse and human monocytes.

1984 ◽  
Vol 159 (3) ◽  
pp. 746-757 ◽  
Author(s):  
J D Loike ◽  
V F Kozler ◽  
S C Silverstein
Keyword(s):  
Creatine Kinase ◽  
Human Lymphocytes ◽  
Creatine Phosphate ◽  
Human Platelets ◽  
In Vitro Cultivation ◽  
Human Monocytes ◽  
Blood Monocytes ◽  
Developmentally Regulated ◽  
The Brain

We have studied the expression of creatine kinase (CK) and the accumulation of creatine phosphate during the differentiation of human and mouse peripheral blood monocytes. Mouse monocytes cultured for 24 h do not contain detectable levels of CK and creatine phosphate. However, resident tissue macrophages and inflammatory elicited macrophages obtained from the peritoneal cavities of mice have 70 and 300 mU per mg protein of CK activity and contain 3 and 6 mol of creatine phosphate per mol of ATP, respectively. The major isozyme of CK in these cells has been identified as the brain form. These findings suggest that the differentiation of monocytes into macrophages is associated with the expression of CK and the accumulation of creatine phosphate. We have found a similar pattern in human monocytes. Human blood monocytes, maintained in culture for 24 or 48 h, do not contain detectable levels of CK or creatine phosphate. Monocyte-derived macrophages (monocytes maintained in tissue cultures for 1 to 2 wk) have up to 100 mU per mg protein of CK activity and contain 0.5 mol of creatine phosphate per mol of ATP. Human macrophages express multiple isozymes of CK including the brain (BB) and possibly the mitochondrial forms of this enzyme. Thus, the expression of CK and the accumulation of creatine phosphate in human monocytes is induced by their in vitro cultivation. The induction of CK during in vitro cultivation occurs independently of the concentration of creatine in the medium. However, the size of the creatine phosphate pool varies with respect to extracellular creatine concentration. Creatine phosphate and CK are not detectable in freshly isolated human lymphocytes, polymorphonuclear leukocytes or erythrocytes, but are found in freshly isolated human platelets.

Characteristics of phosphate-induced Ca2+ efflux from the SR in mechanically skinned rat skeletal muscle fibers

2000 ◽  
Vol 278 (1) ◽  
pp. C126-C135 ◽  
Author(s):  
Adrian M. Duke ◽  
Derek S. Steele
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Muscle Fibers ◽  
Cyclopiazonic Acid ◽  
Creatine Phosphate ◽  
Ruthenium Red ◽  
Rat Skeletal Muscle ◽  
Atpase Inhibitor ◽  
Skeletal Muscle Fibers ◽  
Efflux Pathway

The effects of Pi on sarcoplasmic reticulum (SR) Ca2+ regulation were studied in mechanically skinned rat skeletal muscle fibers. Brief application of caffeine was used to assess the SR Ca2+ content, and changes in concentration of Ca2+([Ca2+]) within the cytosol were detected with fura 2 fluorescence. Introduction of Pi (1–40 mM) induced a concentration-dependent Ca2+ efflux from the SR. In solutions lacking creatine phosphate (CP), the amplitude of the Pi-induced Ca2+ transient approximately doubled. A similar potentiation of Pi-induced Ca2+ release occurred after inhibition of creatine kinase (CK) with 2,4-dinitrofluorobenzene. In the presence of ruthenium red or ryanodine, caffeine-induced Ca2+ release was almost abolished, whereas Pi-induced Ca2+ release was unaffected. However, introduction of the SR Ca2+ ATPase inhibitor cyclopiazonic acid effectively abolished Pi-induced Ca2+ release. These data suggest that Pi induces Ca2+ release from the SR by reversal of the SR Ca2+ pump but not via the SR Ca2+ channel under these conditions. If this occurs in intact skeletal muscle during fatigue, activation of a Ca2+efflux pathway by Pi may contribute to the reported decrease in net Ca2+ uptake and increase in resting [Ca2+].

Myofibrillar end of the creatine phosphate energy shuttle

1984 ◽  
Vol 247 (5) ◽  
pp. C424-C432 ◽  
Author(s):  
F. Savabi ◽  
P. J. Geiger ◽  
S. P. Bessman
Keyword(s):  
Creatine Kinase ◽  
Adenylate Kinase ◽  
Psoas Muscle ◽  
Creatine Phosphate ◽  
Force Of Contraction ◽  
Physiological Concentration ◽  
Complete Relaxation ◽  
Order Of Magnitude ◽  
Contraction And Relaxation

Isometric contraction and relaxation of glycerinated rabbit psoas muscle fibers containing native creatine kinase (CK) and ATPase activities were studied. Energy for contraction and relaxation was provided either by ADP + creatine phosphate (CP) or ATP alone, and the effectiveness of these additions on rate and maximum force of contraction and relaxation were compared. In the presence of 250 microM ADP, physiological concentration of CP (10 mM) produced faster and stronger contraction and faster and more complete relaxation than equimolar or even higher concentrations of ATP. When contraction was initiated by addition of ADP to fibers preincubated with 10 mM CP, the apparent Km for ADP was 1.18 +/- 0.24 mM. If the fibers were preincubated with ADP and contraction initiated by addition of 10 mM CP, the apparent Km for ADP was more than an order of magnitude smaller (76.0 +/- 4 microM). The observed Km for ADP for contraction was about half the Km for CP in solution (151.5 microM). The apparent Km for CP for rate of contraction was 2.67 +/- .046 mM independent of sequence of addition of ADP. Since these experiments were done in the presence of P1,P5-diadenosine 5'-pentaphosphate, a powerful inhibitor of adenylate kinase, the role of this enzyme in the process was not significant. These observations support the idea of compartmentation of myofibrillar CK in close function with myosin ATPase as part of the phosphoryl creatine energy shuttle.

Metabolism of the perfused rabbit heart. V. Verapamil-induced release of creatine kinase

1982 ◽  
Vol 60 (7) ◽  
pp. 952-959 ◽  
Author(s):  
Miguel A. Chiong
Keyword(s):  
Creatine Kinase ◽  
Adenine Nucleotides ◽  
Systolic Pressure ◽  
Creatine Phosphate ◽  
Rabbit Heart ◽  
Left Ventricular ◽  
Calcium Stores ◽  
Ventricular Performance ◽  
Permeability Characteristics ◽  
Energy Stores

The effects of verapamil (VER), at concentrations of 0, 10−9, 10−8, 10−7, and 5 × 10−7 M (or 0, 0.5, 5, 50, and 250 ng/mL) were studied in the isolated rabbit heart during 70 min of aerobic perfusion with a standard Krebs–bicarbonate medium at 37 °C. The studied variables were left ventricular performance (RPP, heart rate times left ventricular (LV) systolic pressure), coronary sinus flow (CSF), oxygen uptake [Formula: see text], rate of creatine kinase (CK) release, and energy stores (glycogen, creatine phosphate (CP), ATP, and total adenine nucleotides (TAN)).The results show that (i) VER depressed RPP in a dose-related manner; (ii) [Formula: see text] declined as VER concentration increased except in the 5 × 10−7 M group which showed a paradoxical increase in O2 uptake; (iii) CSF was only slightly decreased by VER with the exception of the 5 × 10−7 M group, which showed an increase in flow; (iv) VER was associated with increments in the rates of CK release in a dose-related fashion (2, 4, 15, and 29 times the rate observed in the untreated group), and (v) VER was associated with slight decrease in glycogen levels, but no changes in CP or adenine nucleotides.It is concluded that, in our preparation, VER caused marked increases in the rate of CK loss in the absence of depletion of total energy stores. The data suggest that the drug affects the permeability characteristics of the sarcolemma, perhaps via localized depletion of calcium stores.

Brain creatine phosphate and creatine kinase in mice fed an analogue of creatine

1989 ◽  
Vol 483 (1) ◽  
pp. 68-77 ◽  
Author(s):  
David Holtzman ◽  
Eric McFarland ◽  
Timothy Moerland ◽  
Jason Koutcher ◽  
Martin J. Kushmerick ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Creatine Phosphate

scholarly journals Protective effect of creatine against inhibition by methylglyoxal of mitochondrial respiration of cardiac cells

2003 ◽  
Vol 372 (2) ◽  
pp. 661-669 ◽  
Author(s):  
Soumya Sinha ROY ◽  
Swati BISWAS ◽  
Manju RAY ◽  
Subhankar RAY
Keyword(s):  
Creatine Kinase ◽  
Protective Effect ◽  
Mitochondrial Respiration ◽  
Therapeutic Potential ◽  
Ehrlich Ascites Carcinoma ◽  
Creatine Phosphate ◽  
Inhibitory Effect ◽  
Cardiac Cells ◽  
Protective Effects ◽  
Tissue Slices

Previous publications from our laboratory have shown that methylglyoxal inhibits mitochondrial respiration of malignant and cardiac cells, but it has no effect on mitochondrial respiration of other normal cells [Biswas, Ray, Misra, Dutta and Ray (1997) Biochem. J. 323, 343–348; Ray, Biswas and Ray (1997) Mol. Cell. Biochem. 171, 95–103]. However, this inhibitory effect of methylglyoxal is not significant in cardiac tissue slices. Moreover, post-mitochondrial supernatant (PMS) of cardiac cells could almost completely protect the mitochondrial respiration against the inhibitory effect of methylglyoxal. A systematic search indicated that creatine present in cardiac cells is responsible for this protective effect. Glutathione has also some protective effect. However, creatine phosphate, creatinine, urea, glutathione disulphide and β-mercaptoethanol have no protective effect. The inhibitory and protective effects of methylglyoxal and creatine respectively on cardiac mitochondrial respiration were studied with various concentrations of both methylglyoxal and creatine. Interestingly, neither creatine nor glutathione have any protective effect on the inhibition by methylglyoxal on the mitochondrial respiration of Ehrlich ascites carcinoma cells. The creatine and glutathione contents of several PMS, which were tested for the possible protective effect, were measured. The activities of two important enzymes, namely glyoxalase I and creatine kinase, which act upon glutathione plus methylglyoxal and creatine respectively, were also measured in different PMS. Whether mitochondrial creatine kinase had any role in the protective effect of creatine had also been investigated using 1-fluoro-2,4-dinitrobenzene, an inhibitor of creatine kinase. The differential effect of creatine on mitochondria of cardiac and malignant cells has been discussed with reference to the therapeutic potential of methylglyoxal.

Evaluation of a New Procedure for Measuring Serum Creatine Kinase Activity

1970 ◽  
Vol 16 (5) ◽  
pp. 370-374 ◽  
Author(s):  
J Henry Wilkinson ◽  
B Steciw
Keyword(s):  
Creatine Kinase ◽  
Spectrophotometric Method ◽  
Kinase Activity ◽  
Creatine Phosphate ◽  
Sample Volume ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Normal Range ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract A new spectrophotometric microtechnique for the determination of serum creatine kinase activity, in which all reagents are provided in a single com-pressed tablet, has been evaluated. The procedure depends upon coupling the creatine phosphate-ADP reaction with the hexokinase and glucose-6-phosphate dehydrogenase reactions. The new technique is quick, relatively simple, and gives results which compare favorably with the conventional spectrophotometric method in precision and sensitivity. It requires a sample volume of 10 Al, and values ranging from 10 to1600 U/liter can be determined without dilution. Gross hemolysis leads to erroneously high values, but the error is negligible with slightly hemolyzed specimens. A provisional normal range has been established

Perinatal enhancement of cardiac myofibrillar creatine kinase activity without change in enzyme Km

1993 ◽  
Vol 265 (2) ◽  
pp. C375-C378 ◽  
Author(s):  
R. T. Dowell ◽  
M. C. Fu
Keyword(s):  
Creatine Kinase ◽  
Heart Development ◽  
Kinase Activity ◽  
Creatine Phosphate ◽  
Creatine Kinase Activity ◽  
Site Function ◽  
A Subunit ◽  
Michaelis Constants ◽  
Isoenzyme Composition ◽  
Contractile Performance

Myofibrillar creatine kinase (CK) serves as one microcompartment of the phosphorylcreatine shuttle by providing ATP as substrate for adenosinetriphosphatase (ATPase). During perinatal heart development, augmentations of myofibrillar ATPase and CK occur in concert with increased contractile performance. The maximal reaction velocity (Vmax) for CK doubles during development in both intact native myofibril and enzyme extracted from myofibril. The absence of alterations in ADP and creatine phosphate substrate Michaelis constants (Km), isoenzyme composition, or total number of -SH groups suggests active site function (Vmax) is influenced indirectly via a subunit domain effect on enzyme conformation.

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