Journal article
Albumin is a major protein component of transverse tubule vesicles isolated from skeletal muscle
The Journal of biological chemistry, Vol.264(18), pp.10795-10798
1989
DOI: 10.1016/S0021-9258(18)81691-X
PMID: 2732247
Abstract
Despite multiple procedures used to isolate transverse tubule vesicles from rabbit skeletal muscle, few proteins have been identified and shown to be specific to transverse tubule vesicles. Markers for purified transverse tubules have included high affinity dihydropyridine binding, cholesterol content, Mg2+-ATPase activity, (Na+,K+)-ATPase activity, and [3H] ouabain binding. Despite these markers, few proteins from purified transverse tubules can be unequivocally identified using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). In this report we have biochemically and immunologically identified rabbit albumin as a major component of purified transverse tubule membranes from rabbit skeletal muscle. Albumin composed between 5.1 and 9.8% (n = 4) of the total protein in purified transverse tubules based on scans of SDS-PAGE. Furthermore, albumin and other serum proteins are present in preparations of transverse tubules and triads but not in light sarcoplasmic reticulum. Extraction of triads with low concentrations of saponin or sodium dodecyl sulfate completely removes albumin without removing intrinsic membrane proteins. Our results suggest that albumin and other serum proteins are present in the lumen of preparations of transverse tubules and albumin may be used as a marker for the transverse tubules when analyzed on SDS gels.
Details
- Title: Subtitle
- Albumin is a major protein component of transverse tubule vesicles isolated from skeletal muscle
- Creators
- C Michael Knudson - Univ. Iowa coll. medicine, dep. physiology biophysics, Iowa City IA 52242, United StatesKevin P Campbell - Univ. Iowa coll. medicine, dep. physiology biophysics, Iowa City IA 52242, United States
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.264(18), pp.10795-10798
- DOI
- 10.1016/S0021-9258(18)81691-X
- PMID
- 2732247
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- American Society for Biochemistry and Molecular Biology; Bethesda, MD
- Language
- English
- Date published
- 1989
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pathology; Iowa Neuroscience Institute; Radiation Oncology
- Record Identifier
- 9984047866502771
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