About: Carboxyglutamic acid is a research topic. Over the lifetime, 190 publications have been published within this topic receiving 7971 citations. The topic is also known as: Γ-Carboxyglutamic acid.
TL;DR: The identity of gamma-carboxyglutamic acid in the bovine protein was established by mass spectroscopy on the unknown amino acid isolated from alkaline hydrolysates.
Abstract: A gamma-carboxyglutamic acid-containing protein has been purified from the calcified tissues of several vertebrates. The presence of three-gamma-carboxyglutamic acid residues in the bovine protein was established by alkaline hydrolysis and amino acid analysis, a method based upon studies with synthetic gamma-carboxyglutamic acid. The identity of gamma-carboxyglutamic acid in the bovine protein was established by mass spectroscopy on the unknown amino acid isolated from alkaline hydrolysates.
TL;DR: These findings may implicate vitamin K metabolism in normal bone development and suggest a role for the gamma-carboxyglutamate-rich protein in regulation of calcium salt deposition in mineralized tissues.
Abstract: A direct approach has been developed for quantitative identification of the calcium-binding amino acid, gamma-carboxyglutamate, in proteins. This should be advantageous for the study of numerous systems where specific roles for the binding of calcium or other divalent cations are suspected. Investigation of mineralized tissue, where calcium-binding proteins are implicated in the mineralization process, revealed that gamma-carboxyglutamate was present in proteins solubilized from chicken bone with neutral aqueous ethylenediamine tetraacetic acid. This was established by direct isolation of the amino acid from alkaline hydrolysates and its quantitative conversion to glutamic acid by decarboxylation in 0.05 M HCl at 100 degrees. The kinetics of decarboxylation and chromatographic behavior are identical to those of gamma-carboxyglutamate from human prothrombin. After resolution of the soluble bone proteins by phosphate gradient elution from hydroxyapatite, gamma-carboxyglutamate was found to be concentrated primarily in one BaSO4-adsorbable anionic protein species; bone collagen was devoid of the amino acid. In view of the recently discovered requirement of vitamin K for generation of calcium binding sites (gamma-carboxyglutamate) by gamma-carboxylation of specific glutamic acid residues in prothrombin, our findings may implicate vitamin K metabolism in normal bone development and suggest a role for the gamma-carboxyglutamate-rich protein in regulation of calcium salt deposition in mineralized tissues.
TL;DR: A novel protein-mineral complex in the serum of rats treated with doses of the bone-active bisphosphonate etidronate that inhibit normal bone mineralization is discovered, which indicates that the previously reported calcification inhibitory activities of fetuin and MGP may be related to their ability to form stable complexes with nascent mineral nuclei.
TL;DR: In this paper, a chromatographic resolution and quantification of the calcium-binding amino acid γ-carboxyglutamate (Gla) is presented, which is extremely acid labile and totally converted to glutamic acid during acid hydrolysis.
TL;DR: The presence of Gla in soft tissue calcifications is a potentially significant finding, especially in view of its known calcium and phospholipid binding properties as discussed by the authors, since a γ-carboxyglutamic acid-containing protein is normally present in bone and absent in unmineralized tissues.