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PMID: 3609295 Published · ppublish English Journal Article

Salt dependent dimerisation of caldesmon.

FEBS letters ·Vol. 219 ·No. 2 ·1987-07-27 ·Pages 306-10

Cross RA, Cross KE, Small JV

Abstract

Using analytical gel filtration (FPLC) we show here that avian gizzard caldesmon (chain molecular mass 150 kDa) self-associates to form end-to-end dimers. Increasing salt concentration promotes dimerisation: at 150 mM KCl, about 40% of the caldesmon was dimeric. Freshly gel filtered caldesmon had an actin gelating activity which decreased with increasing ionic strength. At 150 mM KCl, caldesmon at a 1:90 molar ratio to actin doubled the low shear viscosity of F-actin. Sixfold less filamin was required to produce the same effect.

MeSH Terms
Animals Calmodulin-Binding Proteins/isolation & purification,metabolism Gizzard, Avian/metabolism Macromolecular Substances Models, Molecular Molecular Weight Muscle, Smooth/metabolism Osmolar Concentration Protein Conformation Turkeys
Chemicals
Calmodulin-Binding Proteins Macromolecular Substances
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cross R A
Cross K E
Small J V
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1987-07-27
Pages
306-10
Language
English
Region
England
NLM ID
0155157
Subset
IM
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