Gc (vitamin D-binding protein) binds the 33.5 K tryptic fragment of actin

Pascal J. Goldschmidt-Clermont; Robert C. Allen; Andre E. Nel; David L. Emerson; Joseph R. Day; Robert M. Galbraith

doi:10.1016/0024-3205(86)90588-6

Gc (vitamin D-binding protein) binds the 33.5 K tryptic fragment of actin

Pascal J. Goldschmidt-Clermont, Robert C. Allen, Andre E. Nel, David L. Emerson, Joseph R. Day, Robert M. Galbraith

Medicine

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Limited proteolysis of G-actin was performed with trypsin and chymotrypsin to compare the binding sites for Gc and DNase. DNase I bound to the N-terminal area corresponding to the major cleavage site on G-actin (residues 62-68) and inhibited proteolysis, but did not bind the 33.5K C-terminal fragment (G-actin_33.5) generated. In contrast, Gc did not exert any inhibitory effect upon proteolysis of the intact native G-actin_42.0 molecule, although its presence protected G-actin_33.5 from further proteolysis. This was shown by gel filtration to be due to the formation of complexes between Gc and G-actin_33.5.

Original language	English (US)
Pages (from-to)	735-742
Number of pages	8
Journal	Life Sciences
Volume	38
Issue number	8
DOIs	https://doi.org/10.1016/0024-3205(86)90588-6
State	Published - Feb 24 1986

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Pharmacology, Toxicology and Pharmaceutics(all)

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@article{6505cc44dc174a699ba60bf3beef2fb4,

title = "Gc (vitamin D-binding protein) binds the 33.5 K tryptic fragment of actin",

abstract = "Limited proteolysis of G-actin was performed with trypsin and chymotrypsin to compare the binding sites for Gc and DNase. DNase I bound to the N-terminal area corresponding to the major cleavage site on G-actin (residues 62-68) and inhibited proteolysis, but did not bind the 33.5K C-terminal fragment (G-actin33.5) generated. In contrast, Gc did not exert any inhibitory effect upon proteolysis of the intact native G-actin42.0 molecule, although its presence protected G-actin33.5 from further proteolysis. This was shown by gel filtration to be due to the formation of complexes between Gc and G-actin33.5.",

author = "Goldschmidt-Clermont, {Pascal J.} and Allen, {Robert C.} and Nel, {Andre E.} and Emerson, {David L.} and Day, {Joseph R.} and Galbraith, {Robert M.}",

year = "1986",

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T1 - Gc (vitamin D-binding protein) binds the 33.5 K tryptic fragment of actin

AU - Goldschmidt-Clermont, Pascal J.

AU - Allen, Robert C.

AU - Nel, Andre E.

AU - Emerson, David L.

AU - Day, Joseph R.

AU - Galbraith, Robert M.

PY - 1986/2/24

Y1 - 1986/2/24

N2 - Limited proteolysis of G-actin was performed with trypsin and chymotrypsin to compare the binding sites for Gc and DNase. DNase I bound to the N-terminal area corresponding to the major cleavage site on G-actin (residues 62-68) and inhibited proteolysis, but did not bind the 33.5K C-terminal fragment (G-actin33.5) generated. In contrast, Gc did not exert any inhibitory effect upon proteolysis of the intact native G-actin42.0 molecule, although its presence protected G-actin33.5 from further proteolysis. This was shown by gel filtration to be due to the formation of complexes between Gc and G-actin33.5.

AB - Limited proteolysis of G-actin was performed with trypsin and chymotrypsin to compare the binding sites for Gc and DNase. DNase I bound to the N-terminal area corresponding to the major cleavage site on G-actin (residues 62-68) and inhibited proteolysis, but did not bind the 33.5K C-terminal fragment (G-actin33.5) generated. In contrast, Gc did not exert any inhibitory effect upon proteolysis of the intact native G-actin42.0 molecule, although its presence protected G-actin33.5 from further proteolysis. This was shown by gel filtration to be due to the formation of complexes between Gc and G-actin33.5.

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