Price N C, Duncan D, Ogg D J
Int J Biochem. 1985;17(7):843-6. doi: 10.1016/0020-711x(85)90275-7.
Phosphoglycerate mutase could be purified to over 95% homogeneity by a single step procedure involving elution from Cibacron Blue-Sepharose by a pulse of cofactor 2,3-bisphosphoglycerate. Although the enzyme has been isolated in only small quantities (c. 100 micrograms), gel filtration and sodium dodecylsulphate polyacrylamide gel electrophoresis indicated that it is monomeric with Mr approximately 23,000, an extremely low value for this enzyme. Preliminary investigations of the kinetic characteristics and the nature of important amino acid side chains have been undertaken.
通过一步操作,用辅因子2,3-二磷酸甘油酸脉冲从Cibacron Blue-Sepharose上洗脱,磷酸甘油酸变位酶可被纯化至超过95%的同质性。尽管该酶仅以少量(约100微克)被分离出来,但凝胶过滤和十二烷基硫酸钠聚丙烯酰胺凝胶电泳表明它是单体,分子量约为23,000,对于这种酶来说这是一个极低的值。已经对其动力学特性和重要氨基酸侧链的性质进行了初步研究。