Gál S, Tar A, Toth-Martinez B L, Hernadi F J
Department of Pharmacology, University Medical School of Debrecen, Hungary.
J Chromatogr. 1991 May 24;545(1):189-95. doi: 10.1016/s0021-9673(01)88707-0.
Simultaneous purification and isoelectric point (pI) determination was carried out at analytical scale of the chromosomal cephalosporinase from the Proteus vulgaris 1028 strain. Comparison of the enzyme to the purification results with m-aminophenylboronic acid-agarose affinity chromatography with sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed that minute amounts of accompanying proteins having identical pI values but different molecular masses were found in the chromatofocused preparation. The molecular mass of the enzyme was 24,000 dalton. The pI was found to be 8.3.
在分析规模下对普通变形杆菌1028菌株的染色体头孢菌素酶进行了同时纯化和等电点（pI）测定。将该酶的纯化结果与间氨基苯硼酸 - 琼脂糖亲和色谱结合十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳进行比较，结果表明在色谱聚焦制剂中发现了微量的伴随蛋白质，它们具有相同的pI值但分子量不同。该酶的分子量为24,000道尔顿。发现其pI为8.3。
