Chan F Y, Torriani A
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
J Bacteriol. 1996 Jul;178(13):3974-7. doi: 10.1128/jb.178.13.3974-3977.1996.
The PstB protein of the phosphate-specific transport (Pst) system of Escherichia coli bound and hydrolyzed ATP, producing ADP. Urea-treated denatured PstB did not bind ATP. The N-terminal amino acid sequence of the immune serum-precipitable PstB protein was determined, and it corresponded to that deduced from the DNA sequence.
大肠杆菌磷酸特异性转运(Pst)系统的PstB蛋白能结合并水解ATP,产生ADP。经尿素处理的变性PstB不结合ATP。测定了免疫血清可沉淀的PstB蛋白的N端氨基酸序列,其与从DNA序列推导的序列一致。