Purification and characterization of calciumbinding protein containing .GAMMA.-carboxyglutamic acid from rat bone.
- 1 January 1980
- journal article
- research article
- Published by Center for Academic Publications Japan in Journal of Nutritional Science and Vitaminology
- Vol. 26 (3) , 209-219
- https://doi.org/10.3177/jnsv.26.209
Abstract
A .gamma.-carboxyglutamic acid (Gla)-containing protein was purified from rat femur cortical bone. The presence of 4 Gla residues in the rat protein was shown by amino acid analysis on alkaline and acid hydrolysates. The protein was extracted from rat cortical bone with 0.5 M EDTA (pH 7.6) and purified from the EDTA extracts by gel filtration on Sephadex G-100 and ion-exchange chromatography on DEAE-Sephadex A-25. The protein has a MW of .apprx. 6000 based on amino acid composition. The protein had 56 amino acid residues containing significant amounts of Asp, Glu and Gla (acidic amino acids). The protein showed Ca-binding activity with Kd = 0.2 mM and Ca-dependent electrophoretic mobility.This publication has 1 reference indexed in Scilit:
- The presence of protein-bound gamma-carboxyglutamic acid in calcium-containing renal calculi.Journal of Clinical Investigation, 1977