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Studies on sarcoplasmic reticulum from slow-twitch muscle

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Summary

Vesicles were isolated from membranes of the sarcoplasmic reticulum (SR) of rabbit slow-twitch muscle by differential and sucrose density gradient centrifugation after homogenization. In some experiments, the vesicles were further fractionated by loading them with calcium oxalate followed by centrifugation in a sucrose density gradient.

Protein composition of the isolated vesicles was complex and differed from the protein composition of fast-twitch muscle vesicles. However, other protein components, which were also present in fast-twitch muscle SR vesicles, have been identified: Ca2+-dependent ATPase, calsequestrin, 160 000 molecular weight glycoprotein and 53 000 molecular weight glycoprotein. The amount of the Ca2+-dependent ATPase and calsequestrin was several times lower in the slow-twitch muscle SR vesicles. This has been observed in both the original and the loaded vesicles.

The slow-twitch muscle SR vesicles showed active calcium transport, Ca2+-dependent ATPase activity, and the formation of the phosphorylated intermediate under conditions similar to those established for fast-twitch muscle SR. However, these activities, when expressed per mg of total protein, were several times lower than the analogous activities in the SR vesicles isolated from fast-twitch skeletal muscle. When the same enzyme activities were expressed per mg of the 105 000 molecular weight ATPase, the values obtained were very similar in both kinds of vesicles.

The results indicate that the slow rate of calcium transport, found in slow-twitch muscle SR vesicles, may be related to a low content of the calcium-transporting ATPase in the membrane.

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Abbreviations

Acid phosphatase:

Orthophosphoric monoester phosphohydrolase (EC 3.1.3.2)

ATP:

Adenosine triphosphate

ATPase:

Adenosine triphosphatase (EC 3.6.1.3)

DFP:

Di-isopropylfluorophosphate

EGTA:

Ethylene glycol bis (β-aminoethyl ether)-N′,N′-tetraacetic acid

ENDO H:

ENDO-B-N-acetylglucosaminidase H (Streptomyces griseus) (Health Research, Inc., Albany, New York, U.S.A.)

Glucose-6-phosphatase:

d-Glucose-6-phosphate phosphorylase (EC 3.1.3.9)

5′-Nucleotidase:

5′-Ribonucleotide phosphohydrolase (EC 3.1.3.5)

PMSF:

Phenylmethyl sulphonylfluoride

Phosphorylaseb :

Glycogen phosphorylaseb (EC 2.4.1.1)

SDS:

Sodium dodecyl sulphate

Stains-all:

[1-Ethyl-2-[3-(1-ethylnaphthol[1,2d]thiazolin-2-ylidene)-2-methylpropenyl]-naphthol[1,2d]-thiazolium bromide (Kodak Organic Chemicals)

Succinate dehydrogenase:

succinate cytochromec reductase (EC 1.3.3.99.1)

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  1. Elzbieta Zubrzycka-Gaarn

    Present address: Banting and Best Department of Medical Research, C.H. Best Institute, University of Toronto, 112 College Street, M5G 1L6, Toronto, Ontario, Canada

Authors and Affiliations

  1. Department of Biochemistry of Nervous System and Muscle, Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093, Warszawa, Poland

    Elzbieta Zubrzycka-Gaarn, Bozena Korczak, Hanna Osinska & M. G. Sarzala

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  1. Elzbieta Zubrzycka-Gaarn
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  2. Bozena Korczak
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  3. Hanna Osinska
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  4. M. G. Sarzala
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Zubrzycka-Gaarn, E., Korczak, B., Osinska, H. et al. Studies on sarcoplasmic reticulum from slow-twitch muscle. J Muscle Res Cell Motil 3, 191–212 (1982). https://doi.org/10.1007/BF00711942

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