The small molecular weight, gamma-carboxyglutamic acid-containing protein of rabbit bone tissue.
The major gamma-carboxyglutamic acid-containing protein of rabbit cortical bone isolated and purified from near-neutral (pH 7.5) EDTA-extracts by DEAE-cellulose and Sephadex G 75 column chromatography had a molecular weight of about 5600 based on integral amino-acid composition; this was confirmed by high-performance liquid chromatography. The purified protein had high glutamic acid and aspartic-acid contents, two to three residues of gamma-carboxyglutamic acid per molecule and zero levels of serine, threonine, methionine, histidine and tryptophan. Equilibrium dialysis indicated that the protein has a weak affinity for calcium ions with a formation constant of 1515 M-1 at I 0.15, pH 7.5, 25 degrees C with a binding capacity of 2 mol calcium per mole protein.
D015055:1-Carboxyglutamic Acid / Q000302:isolation & purification* / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001842:Bone and Bones / Q000032:analysis*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005971:Glutamates / Q000302:isolation & purification*; D008970:Molecular Weight; D011485:Protein Binding; D011817:Rabbits
D000596:Amino Acids; D005971:Glutamates; D015055:1-Carboxyglutamic Acid