Studies of solubilized sarcoplasmic reticulum

B. H. McFarland, G. Inesi

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

The non-ionic detergent Triton X-100 solubilizes most of the protein and phospholipid from the sarcoplasmic reticulum of rabbit skeletal muscle. The calcium dependent ATPase of the sarcoplasmic reticulum is found in the soluble fraction whereas the basic ATPase activity remains insoluble in Triton X-100. Analytical ultracentrifugation and disc electrophoresis indicate that the solubilized material consists of particles having a molecular weight of approximately 80,000 daltons. These particles have a strong tendency to aggregate.

Original languageEnglish (US)
Pages (from-to)239-243
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume41
Issue number1
DOIs
StatePublished - Oct 9 1970

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Studies of solubilized sarcoplasmic reticulum'. Together they form a unique fingerprint.

  • Cite this