Takagi T, Suzuki M, Baba T, Minegishi K, Sasaki S
Biochem Biophys Res Commun. 1984 Jun 15;121(2):592-7. doi: 10.1016/0006-291x(84)90223-7.
Pure amelogenin protein in developing bovine incisor enamel was isolated and its primary structure was investigated by sequencing the peptides obtained after clostripain and chymotrypsin digestions and CNBr degradation with an automated Edman sequencer. The enamel protein was found to be composed of 170 amino acid residues with one phosphate having a molecular weight of 19,350 and its complete amino acid sequence was elucidated. This protein has no sequence homology with any other tissue or secretory protein of known structure.
从发育中的牛切牙釉质中分离出纯釉原蛋白，并通过用自动Edman测序仪对梭菌蛋白酶和胰凝乳蛋白酶消化以及溴化氰降解后获得的肽进行测序，研究其一级结构。发现该釉质蛋白由170个氨基酸残基组成，带有一个磷酸基团，分子量为19,350，并阐明了其完整的氨基酸序列。该蛋白与已知结构的任何其他组织或分泌蛋白均无序列同源性。
