Literature DB >> 6236806

The interaction of calmodulin with human and avian spectrin.

A Husain, G J Howlett, W H Sawyer.   

Abstract

An air-driven ultracentrifuge was used to investigate the calcium-dependent interaction of 125I-calmodulin with human and avian spectrins. The equilibrium constants (Ka) for the interaction between calmodulin and human spectrin dimer and tetramer under non-denaturing conditions were estimated to be 4.6 X 10(4) M-1 and 7.3 X 10(4) M-1, respectively. The denaturation of human spectrin by urea (5 M) increased the Ka for calmodulin to 4.6 X 10(5) M-1. The value of Ka for the interaction of calmodulin with avian spectrin dimer under non-denaturing conditions was 5.1 X 10(5) M-1. A bifunctional reagent cross-linked both avian spectrin and human spectrin to calmodulin in a calcium-dependent manner.

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Year:  1984        PMID: 6236806     DOI: 10.1016/0006-291x(84)91218-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Spin label study of erythrocyte deformability. Ca2+-induced loss of deformability and the effects of stomatocytogenic reagents on the deformability loss in human erythrocytes in shear flow.

Authors:  S Noji; S Taniguchi; H Kon
Journal:  Biophys J       Date:  1987-08       Impact factor: 4.033

Review 2.  Role of the phosphorylation of red blood cell membrane proteins.

Authors:  P Boivin
Journal:  Biochem J       Date:  1988-12-15       Impact factor: 3.857

3.  Spin-labeling studies of the conformation of the Ca(2+)-regulatory protein calmodulin in solution and bound to the membrane skeleton in erythrocyte ghosts: implications to transmembrane signaling.

Authors:  M A Yacko; D A Butterfield
Journal:  Biophys J       Date:  1992-08       Impact factor: 4.033

  3 in total

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