Purification and characterization of calciumbinding protein containing .GAMMA.-carboxyglutamic acid from rat bone.
1980; Center for Academic Publications Japan; Volume: 26; Issue: 3 Linguagem: Inglês
10.3177/jnsv.26.209
ISSN1881-7742
AutoresYoko Otawara, Norimasa HOSOYA, Hisataka Kasai, Norio Okuyama, Sachiko MORIUCHI,
Tópico(s)Muscle metabolism and nutrition
ResumoA γ-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 molecular weight of about 6, 000 on the basis of amino acid composition. The protein had 56 amino acid residues containing significant amounts of Asp, Glu, and Gla (acidic amino acids). The protein showed calcium-binding activity with Kd=0.2 mM and calcium-dependent electrophoretic mobility.
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