Some properties of creatine phosphokinase

Ennor, A. H.; Rosenberg, H.

doi:10.1042/bj0570203

Cited by 116 publications

(21 citation statements)

References 6 publications

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“…The high sensitivity of creatine kinase to SH-group modifications has been known for more than 30 years [28]. Creatine kinase has eight SH-groups, two of which per dimer are more reactive to thiol-blocking reagents and are therefore believed to be essential for the activity of the enzyme [29].…”

Section: Discussionmentioning

confidence: 99%

Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca²⁺‐ATPase

Kôrge

Byrd

Campbell

1993

European Journal of Biochemistry

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We investigated the role of creatine kinase bound to sarcoplasmic reticulum membranes of fast skeletal muscle in the local regeneration of ATP and the possible physiological significance of this regeneration for calcium pump function. Our results indicate that ADP produced by sarcoplasmic reticulum Ca2+-ATPase is effectively phosphorylated by creatine kinase in the presence of creatine phosphate. This phosphorylation is an important function of the membrane-bound creatine kinase because accumulation of ADP has a depressive effect on Ca2+-uptake by sarcoplasmic reticulum vesicles. The concentration-dependent depression of Ca2+-uptake by ADP was especially pronounced when there was strong back inhibition by high intravesicular [Ca"]. ATP regenerated by endogenous creatine kinase was not in free equilibrium with the ATP in the surrounding medium, but was used preferentially by Ca2+-ATPase for Ca2+-uptake. Efficient translocation of ATP from creatine kinase to Ca2+-ATPase, despite the presence of an ATP trap in the surrounding medium, can be explained by close localization of creatine kinase and Ca2+-ATPase on the sarcoplasmic reticulum membranes. These results suggest the existence of functional coupling between creatine kmase and Ca2+-ATPase on skeletal muscle sarcoplasmic reticulum membranes. Several factors (amount of membrane-bound creatine kinase, oxidation of SH groups of creatine kinase, decrease in [phosphocreatine]) can influence the ability of creatine kinase/phosphocreatine system to support a low ADP/ATP ratio and fuel the Ca2+-pump with ATP. These factors may become operative in the living cells, influencing functional coupling between creatine kinase and Ca2+-ATPase and may have an indirect effect on Ca2+-pump function before Ca2+-ATPase itself is affected.There is ample published evidence to suggest that ATP resynthesis can occur locally on myofibrills and biomembranes due to the activity of creatine kinase and glycolytic enzymes bound to myofibrills [l -41, sarcoplasmic reticulum (SR) [5-81 and plasma membranes [8-lo]. The existence of site-specific regeneration of ATP, which creates a local pool of ATP in the close vicinity of sites of ATP utilization, provides an explanation for numerous findings where changes in myofibrillar function did not correlate with the cytosolic [ATP] or ATP level in the media [l, 3, 11-13]. Reversible binding of creatine kinase to cardiac and skeletal muscle myofibrils and the involvement of this bound creatine kinase in the energy supply for contraction has been demonstrated in several laboratories [l -41. Recently, creatine kinase has been shown to be attached to highly purified SR membranes from skeletal muscle [5]. These results confirmed earlier findings [6, 71, which demonstrated that creCorrespondence to P. Korge,

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Section: Discussionmentioning

confidence: 99%

Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca²⁺‐ATPase

Kôrge

Byrd

Campbell

1993

European Journal of Biochemistry

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“…by the method of Ennor and Rosenberg (1954). The detailed procedure was similar to that used by Hughes (1962) with the following modifications: 1 A lower concentration (4-2 mM) of cysteine was used in the medium, since this was found to be adequate for maximum activity: 2 To avoid the appearance of turbidity which was occasionally encountered during the creatine determination, the pchloromercuribenzoate was added at a later stage.…”

Section: Methodsmentioning

confidence: 99%

Serum enzyme studies in muscle disease: Part I Variations in serum creatine kinase activity in normal individuals

Pearce¹,

Pennington²,

Walton³

1964

Journal of Neurology, Neurosurgery & Psychiatry

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It has been recognized for many years that in patients with muscular dystrophy there are substantial increases in the activity of certain enzymes, e.g., aldolase and the transaminases, in the serum. Extensive surveys by several workers have shown that the changes are particularly striking in cases of the Duchenne type muscular dystrophy (decreasing as the disease progresses), smaller in the limb-girdle and facio-scapulo-humeral types of dystrophy, and slight or absent in cases of neurogenic muscular weakness and wasting (Dreyfus and Schapira,

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“…Substances without effect, and those found to interfere with the colour development, are listed in Table 1. The interference by 1 mM-sodium thioglycollate was completely eliminated after reaction with the p-chloromercuribenzoic acid in the inhibitor mixture, as described by Ennor & Stocken (1948).…”

Section: Resultsmentioning

confidence: 99%

“…The pH-rate curves (Fig. 2) for the forward and reverse reactions were similar in shape and appearance to those of the muscle enzyme, save that the brain enzyme in glycylglycine buffer had a pH optimum for the reverse reaction of 7-9, compared with a pH optimum of 7 0 for the muscle enzyme with magnesium as an activating ion (Kuby et al 1954b) and 7-2 with calcium as the activating ion (Ennor & Rosenberg, 1954 Nihei et al (1961) this point could represent the pK of a dissociating group on the enzyme-substrate complex, possibly an amino group. The enzyme was found to be stable over 8 min.…”

Section: Withoutmentioning

confidence: 99%

“…Contradictory reports (Kuby et al 1954a;Ennor & Rosenberg, 1954;Oliver, 1955;Cho, Haslett & Jenden, 1960; have appeared on the activation of the muscle enzyme by thiols and the phenomenon does not seem to have been easy to observe. By contrast, complete inactivation and reactivation of concentrated preparations of the partially purified brain enzyme has been noted on several occasions.…”

Section: )mentioning

confidence: 99%

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Adenosine Triphosphate-Creatine Phosphotransferase From Ox Brain. 2. Properties and Function

Wood¹

1963

Biochemical Journal

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Some properties of creatine phosphokinase

Cited by 116 publications

References 6 publications

Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca²⁺‐ATPase

Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca²⁺‐ATPase

Serum enzyme studies in muscle disease: Part I Variations in serum creatine kinase activity in normal individuals

Adenosine Triphosphate-Creatine Phosphotransferase From Ox Brain. 2. Properties and Function

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Some properties of creatine phosphokinase

Cited by 116 publications

References 6 publications

Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca2+‐ATPase

Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca2+‐ATPase

Serum enzyme studies in muscle disease: Part I Variations in serum creatine kinase activity in normal individuals

Adenosine Triphosphate-Creatine Phosphotransferase From Ox Brain. 2. Properties and Function

Contact Info

Product

Resources

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Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca²⁺‐ATPase

Functional coupling between sarcoplasmic‐reticulum‐bound creatine kinase and Ca²⁺‐ATPase