Characterization of calcium binding to brain spectrinShow full item record
Title | Characterization of calcium binding to brain spectrin |
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Author | Wallis, C. J.; Wenegieme, Elizabeth F.; Babitch, Joseph A. |
Date | 1992 |
Abstract | Brain spectrin alpha and beta chains bind 45Ca2+, as shown by the calcium overlay method. Flow dialysis measurements revealed eight high affinity binding sites/tetramer that comprise two binding components (determined by nonlinear regression analysis). The first component has one or two sites (kd = 2-30 x 10(-8) M), depending on the ionic strength of the binding buffer, with the remaining high affinity sites in the second component (kd = 1-3 x 10(-6) M). In addition, there is a variable, low affinity binding component (n = 100-400, kd = 1-2 x 10(-4) M). Magnesium inhibits calcium binding to the low affinity sites with a K1 = 1.21 mM. Proteolytic fragments from trypsin or chymotrypsin digests of brain spectrin bind 45Ca2+ if they include alpha domain IV, alpha domain III, or the amino-terminal half of the beta chain (but more than 25 kDa from the amino-terminal). These data suggest that calcium ions bind with high affinity to the putative EF-hands in alpha domain IV and to one site in the amino-terminal half of the beta chain that is associated with alpha domain IV in the native dimer. The localization is consistent with a direct calcium modulation of the spectrin-actin-protein 4.1 interaction. In addition, there appears to be one high affinity site near the hypersensitive region of alpha brain spectrin. All four proposed binding sites occur near probable calmodulin-binding or calcium-dependent protease cleavage sites. |
Link | https://doi.org/10.1016/s0021-9258(18)42839-6
https://repository.tcu.edu/handle/116099117/56606 |
Department | Chemistry and Biochemistry |
Subject | Binding site
Biophysics Chemistry Protease Chymotrypsin Tetramer Trypsin Spectrin Calcium Biochemistry Dissociation constant Animals Autoradiography Binding Sites Blotting, Western Brain/metabolism Calcium/metabolism Calmodulin/metabolism Cations, Divalent Cattle Chymotrypsin/metabolism Electrophoresis, Polyacrylamide Gel Horses Hydrolysis Osmolar Concentration Spectrin/metabolism Trypsin/metabolism |
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