Studies of solubilized sarcoplasmic reticulum

Bentson McFarland, G. Inesi

Research output: Contribution to journalArticle

24 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Octoxynol
Sarcoplasmic Reticulum
Adenosine Triphosphatases
Sarcoplasmic Reticulum Calcium-Transporting ATPases
Disc Electrophoresis
Ultracentrifugation
Electrophoresis
Detergents
Muscle
Phospholipids
Skeletal Muscle
Molecular Weight
Molecular weight
Rabbits
Calcium
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Studies of solubilized sarcoplasmic reticulum. / McFarland, Bentson; Inesi, G.

In: Biochemical and Biophysical Research Communications, Vol. 41, No. 1, 09.10.1970, p. 239-243.

Research output: Contribution to journalArticle

McFarland, Bentson ; Inesi, G. / Studies of solubilized sarcoplasmic reticulum. In: Biochemical and Biophysical Research Communications. 1970 ; Vol. 41, No. 1. pp. 239-243.
@article{a0f3239ad7534506aa394563019bb0eb,
title = "Studies of solubilized sarcoplasmic reticulum",
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.",
author = "Bentson McFarland and G. Inesi",
year = "1970",
month = "10",
day = "9",
doi = "10.1016/0006-291X(70)90494-8",
language = "English (US)",
volume = "41",
pages = "239--243",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Studies of solubilized sarcoplasmic reticulum

AU - McFarland, Bentson

AU - Inesi, G.

PY - 1970/10/9

Y1 - 1970/10/9

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0014938375&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014938375&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(70)90494-8

DO - 10.1016/0006-291X(70)90494-8

M3 - Article

VL - 41

SP - 239

EP - 243

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -