Gc (vitamin D-binding protein) binds the 33.5 K tryptic fragment of actin |
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| Authors: | P J Goldschmidt-Clermont R C Allen A E Nel D L Emerson J R Day R M Galbraith |
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| Institution: | 1. Burn Centre and General Intensive Care Department, University of Liège, University Hospital, Sart-Tilman, Liège, Belgium;2. Anesthesiology Department, University of Liège, University Hospital, Sart-Tilman, Liège, Belgium;3. Clinical Chemistry Department, University of Liège, University Hospital, Sart-Tilman, Liège, Belgium;4. Nephrology Department, University of Liège, University Hospital, Sart-Tilman, Liège, Belgium;1. Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA, United States;2. Clinical Laboratories, University of Pittsburgh Medical Center Presbyterian and Shadyside Hospitals, Pittsburgh, PA, United States;3. McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, PA, United States;4. Clinical Laboratory, Children''s Hospital of Pittsburgh of UPMC, Pittsburgh, PA, United States;1. Clinical Analysis and Biochemistry Department, Germans Trias i Pujol University Hospital, Badalona, Universitat Autònoma Barcelona, Spain;2. Paediatrics Department, Germans Trias i Pujol University Hospital, Badalona, Universitat Autònoma Barcelona, Spain;1. From the Division of Endocrinology, Metabolism & Nutrition, Department of Medicine, Rutgers-Robert Wood Johnson Medical School, New Brunswick, New Jersey;2. Department of Nutritional Sciences, Rutgers University, New Brunswick, New Jersey |
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| 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. |
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