Shimomura H, Kanai Y, Sanada K
J Biochem. 1984 Aug;96(2):405-11. doi: 10.1093/oxfordjournals.jbchem.a134851.
A bone Gla-containing protein (osteocalcin) of cat has been isolated and the complete primary structure has been determined to be YLAPGLGAOAPYPDPLXPKRXICXLNPDCDELADHIGFQDAYRRFYGTV. The protein consists of 49 amino acid residues (Mr. 5,641) containing three Gla residues and a single disulfide bond. Although the C-terminal 30 residues (20th to 49th) of the sequences of cow, monkey, and human osteocalcins are identical, three amino acid substitutions occur at positions 22, 40, and 48 in the case of cat. These substitutions can be explained by single point mutations.
已分离出猫的一种含骨γ-羧基谷氨酸蛋白（骨钙素），并确定其完整的一级结构为YLAPGLGAOAPYPDPLXPKRXICXLNPDCDELADHIGFQDAYRRFYGTV。该蛋白由49个氨基酸残基组成（分子量5641），含有三个γ-羧基谷氨酸残基和一个二硫键。尽管牛、猴和人骨钙素序列的C末端30个残基（第20至49位）是相同的，但猫的序列在第22、40和48位发生了三个氨基酸替换。这些替换可以用单点突变来解释。
