Specific protein-protein interactions of calsequestrin with junctional sarcoplasmic reticulum of skeletal muscle

Journal Article · Thu Nov 15 00:00:00 EST 1990 · Biochemical and Biophysical Research Communications; (USA)

DOI:https://doi.org/10.1016/0006-291X(90)91584-F· OSTI ID:6276014

Damiani, E; Margreth, A ^[1]

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1. Universita' di Padova (Italy)

Minor protein components of triads and of sarcoplasmic reticulum (SR) terminal cisternae (TC), i.e. 47 and 37 kDa peptides and 31-30 kDa and 26-25 kDa peptide doublets, were identified from their ability to bind {sup 125}I calsequestrin (CS) in the presence of EGTA. The CS-binding peptides are specifically associated with the junctional membrane of TC, since they could not be detected in junctional transverse tubules and in longitudinal SR fragments. The 31-30 kDa peptide doublet, exclusively, did not bind CS in the presence of Ca{sup 2+}. Thus, different types of protein-protein interactions appear to be involved in selective binding of CS to junctional TC.

• OSTI ID: 6276014
• Journal Information: Biochemical and Biophysical Research Communications; (USA), Vol. 172:3; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
MUSCLES
BIOCHEMISTRY
PEPTIDES
BIOCHEMICAL REACTION KINETICS
CALCIUM COMPOUNDS
CELL MEMBRANES
CHICKENS
EGTA
RABBITS
SARCOPLASMIC RETICULUM
TRACER TECHNIQUES
ALCOHOLS
ALKALINE EARTH METAL COMPOUNDS
ANIMALS
BIRDS
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CHELATING AGENTS
CHEMISTRY
ENDOPLASMIC RETICULUM
FOWL
GLYCOLS
HYDROXY COMPOUNDS
ISOTOPE APPLICATIONS
KINETICS
MAMMALS
MEMBRANES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANOIDS
PROTEINS
REACTION KINETICS
VERTEBRATES
550201* - Biochemistry- Tracer Techniques