CHARACTERIZATION OF A GAMMA-CARBOXYGLUTAMIC ACID-CONTAINING PROTEIN FROM BONE
CHARACTERIZATION OF A GAMMA-CARBOXYGLUTAMIC ACID-CONTAINING PROTEIN FROM BONE
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DOI:
10.1073/pnas.73.5.1447
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发表时间:
1976-01-01
影响因子:
11.1
通讯作者:
RAMAN, N
中科院分区:
文献类型:
--
作者:
PRICE, PA;OTSUKA, AS;RAMAN, N
A .gamma.-carboxyglutamic acid-containing protein was purified from several calcified tissues. The presence of 3 .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. The protein is extracted from finely ground bone during demineralization with EDTA, and purified from EDTA extracts by gel filtration over Sephadex G-100 and chromatography on DEAE-Sephadex. The protein has a 6800 MW and an isoelectric point of pH 3.7. The amino-terminal 15 residues were determined, and establish that this protein is not a fragment of the .gamma.-carboxyglutamic acid-containing blood clotting factors. Similar .gamma.-carboxyglutamic acid-containing proteins also were purified from bovine dentine, swordfish vertebrae, and human tibia. No .gamma.-carboxyglutamic acid can be detected in the calcified cartilage of elasmobranches, in calf epiphyseal growth cartilage, or in bovine tooth enamel. The bovine protein binds strongly to hydroxyapatite but not to amorphous calcium phosphate, and it is a potent inhibitor of hydroxyapatite crystallization from supersaturated solutions of Ca and phosphate.