Exchange of calcium between muscle Ca2+-binding proteins

Hans J. Moeschler, Dean A. Malencik, Sitivad Pocinwong, Olusola Alaba, W. Glenn Kerrick, Edmond H. Fischer

Research output: Contribution to journalArticle

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Abstract

Sarcoplasmic reticulum isolated from skeletal muscle of the rabbit and the Pacific dogfish (Squalus acanthias) was characterized in terms of its Ca2+-uptake at different temperatures. SR from both species showed comparable Ca2+-uptake rates at their basal body temperatures (5°C and 37°C, respectively). Only very low percentages of phosphorylase, phosphorylase kinase and phosphatase were found to be associated with the purified vesicles, once these were freed of contaminating glycogen particles. Ca2+-fluxes during contraction/relaxation-cycles in muscles were studied in a reconstituted system by measuring the inhibition of the rate of Ca2+-uptake by the sarcoplasmic reticulum and of the Ca2+-dependent activity of phosphorylase kinase, respectively, by metal-free troponin, troponin-C, parvalbumin and phosphorylase kinase; EGTA was used as an internal standard. Ca2+-binding capacities of the various proteins were determined separately by gel filtration experiments. Data obtained agreed with published values for troponin, troponin-C and parvalbumin; for phosphorylase kinase, a value of n- = 8 was found regardless of the state of phosphorylation of the enzyme. Results obtained from both types of experiments established apparent Ca2+-affinities in the following decreasing order : phosphorylase kinase ∼ parvalbumin > EGTA > troponintroponin-C, with no difference found between the non-phosphorylated and phosphorylated forms of phosphorylase kinase. Apparent equilibrium constants for these Ca2+-complexes, relative to EGTA, were in agreement with published values obtained from classical equilibrium studies. Similar results were obtained with proteins isolated from rabbit and dogfish muscle. No indication of protein-protein interactions affecting Ca2+-fluxes could be found in such a reconstituted system, except for the singular case of a slight increased inhibition of phosphorylase kinase by parvalbumin following phosphorylation of the enzyme.

Original languageEnglish
Pages (from-to)615-624
Number of pages10
JournalBiochimie
Volume61
Issue number5-6
DOIs
StatePublished - Sep 10 1979
Externally publishedYes

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Phosphorylase Kinase
Muscle
Parvalbumins
Carrier Proteins
Calcium
Muscles
Egtazic Acid
Dogfish
Troponin C
Phosphorylation
Troponin
Sarcoplasmic Reticulum
Proteins
Squalus acanthias
Fluxes
Rabbits
Phosphorylases
Equilibrium constants
Enzymes
Body Temperature

ASJC Scopus subject areas

  • Biochemistry

Cite this

Moeschler, H. J., Malencik, D. A., Pocinwong, S., Alaba, O., Kerrick, W. G., & Fischer, E. H. (1979). Exchange of calcium between muscle Ca2+-binding proteins. Biochimie, 61(5-6), 615-624. https://doi.org/10.1016/S0300-9084(79)80159-5

Exchange of calcium between muscle Ca2+-binding proteins. / Moeschler, Hans J.; Malencik, Dean A.; Pocinwong, Sitivad; Alaba, Olusola; Kerrick, W. Glenn; Fischer, Edmond H.

In: Biochimie, Vol. 61, No. 5-6, 10.09.1979, p. 615-624.

Research output: Contribution to journalArticle

Moeschler, HJ, Malencik, DA, Pocinwong, S, Alaba, O, Kerrick, WG & Fischer, EH 1979, 'Exchange of calcium between muscle Ca2+-binding proteins', Biochimie, vol. 61, no. 5-6, pp. 615-624. https://doi.org/10.1016/S0300-9084(79)80159-5
Moeschler HJ, Malencik DA, Pocinwong S, Alaba O, Kerrick WG, Fischer EH. Exchange of calcium between muscle Ca2+-binding proteins. Biochimie. 1979 Sep 10;61(5-6):615-624. https://doi.org/10.1016/S0300-9084(79)80159-5
Moeschler, Hans J. ; Malencik, Dean A. ; Pocinwong, Sitivad ; Alaba, Olusola ; Kerrick, W. Glenn ; Fischer, Edmond H. / Exchange of calcium between muscle Ca2+-binding proteins. In: Biochimie. 1979 ; Vol. 61, No. 5-6. pp. 615-624.
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