Ozegowski J H, Günther E, Vettermann S, Müller P J, Wollweber L
Institut für Experimentelle Mikrobiologie, Friedrich-Schiller-Universität Jena (FSU), Germany.
Zentralbl Bakteriol. 1998 Jul;288(1):13-21. doi: 10.1016/s0934-8840(98)80092-3.
A low molecular weight mitogen (LMP) from Streptococcus pyogenes strain NY 5 was successively purified by adsorption on phenylsepharose, chromatography on Resource S and Superdex G 30 and finally by affinity chromatography on antiphosphothreonine agarose. The N-terminal protein sequence of the mitogen was determined. The occurrence of phosphoamino acids was investigated by immunoassay using monoclonal antibodies. The LMP is a threonine-phosphorylated protein different of HPR protein of PTS-system, its mitogenic activity was lost after treatment with streptococcal protein phosphatase or alkaline phosphatase. The inactivated LMP was activated by phosphorylation with phosphokinase and ATP. The active LMP was also inactivated in streptococcal cultures secreting acid protein phosphatase during the phase of phosphate limitation.
从化脓性链球菌NY 5菌株中提取的一种低分子量促细胞分裂剂(LMP),先后通过苯基琼脂糖吸附、Resource S和Superdex G 30色谱法,最后通过抗磷酸苏氨酸琼脂糖亲和色谱法进行纯化。测定了该促细胞分裂剂的N端蛋白质序列。使用单克隆抗体通过免疫测定法研究了磷酸氨基酸的存在情况。该LMP是一种苏氨酸磷酸化蛋白,与磷酸转移酶系统的HPR蛋白不同,用链球菌蛋白磷酸酶或碱性磷酸酶处理后,其促有丝分裂活性丧失。失活的LMP通过磷酸激酶和ATP磷酸化而被激活。在磷酸盐限制阶段,分泌酸性蛋白磷酸酶的链球菌培养物中,活性LMP也会失活。