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Salt dependent dimerisation of caldesmon
Author(s) -
Cross R.A.,
Cross K.E.,
Small J.V.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80241-7
Subject(s) - caldesmon , chemistry , actin , filamin , biophysics , salt (chemistry) , size exclusion chromatography , molecular mass , fast protein liquid chromatography , crystallography , chromatography , biochemistry , calmodulin , cytoskeleton , high performance liquid chromatography , organic chemistry , biology , cell , enzyme
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.