Arai M, Abe K, Yamato I
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
Biochem Int. 1992 Jul;27(2):275-9.
HPr protein, the ptsH gene product, of the phosphoenolpyruvate:sugar phosphotransferase system of Pediococcus halophilus was purified to homogeneity using heat and acid treatments, DEAE-Sepharose CL-6B and hydroxyapatite column chromatographies. The purified protein complemented the HPr activity of the phosphotransferase system in Staphylococcus aureus ptsH mutant cell lysate. The molecular weight was estimated as 6,500 by SDS polyacrylamide gel electrophoresis. The amino acid sequence of the amino-terminal part (1-44) of the native purified protein was highly homologous to those of HPr proteins from gram-positive bacteria. Antiserum raised against the purified HPr protein specifically reacted with the Pediococcus halophilus HPr protein and did not cross-react with Staphylococcus aureus or Escherichia coli HPr proteins.
糖磷酸转移酶系统的HPr蛋白（ptsH基因产物）通过加热和酸处理、DEAE-琼脂糖CL-6B和羟基磷灰石柱色谱法纯化至同质。纯化后的蛋白补充了金黄色葡萄球菌ptsH突变体细胞裂解物中磷酸转移酶系统的HPr活性。通过SDS聚丙烯酰胺凝胶电泳估计分子量为6500。天然纯化蛋白氨基末端部分（1-44）的氨基酸序列与革兰氏阳性菌的HPr蛋白高度同源。针对纯化的HPr蛋白产生的抗血清与嗜盐片球菌HPr蛋白特异性反应，但不与金黄色葡萄球菌或大肠杆菌的HPr蛋白发生交叉反应。
