狨猴(Saguinus mystax)血红蛋白(Hb)α链一级结构的测定

THE PRIMARY STRUCTURE OF HEMOGLOBIN a CHAIN OF MARMOSET (Saguinus mystax)

分析了狨猴(Saguinus mystax)血红蛋白(Hb)a链的氨基酸序列.经CM-23纤维素柱层析得到的狨猴Hb珠蛋白a链,分别用溴化氰裂解、胰蛋白酶和糜蛋白酶消化,经高效液相层析(HPLC)和高压电泳-纸层析分离后的肽段,用蛋白质顺序自动分析仪测定其氨基酸序列.结果表明,完整狨猴a链的一级结构与人、恒猴和懒猴的a链有差异,肯定了狨猴的进化地位.同时对测定一级结构的方法进行了讨论.

a Chain of hemoglobin from Saguinus mystax was isolated by CM-23 cellulose column chromatography. Desalted a Chain was cleaved by cyanogen bromide, TPCK-trypsin and chymotrypsin respectively. Peptides were isolated and purified by HPLC and high voltage electrophoresis-paper chromatography. Peptide sequencing was done by Model 470 gas phase protein sequencer and DNS-Cl method. The complete amino acid sequence of hemoglobin a chain of Saguinus mystax was compared with that of human, Macaca mulatta and Nycticebus coucang. The evolutionary status of Saguinus mystax and experimental strategy of protein sequencing were discussed.