title: Polyphosphate-glucose phosphotransferase. Purification of Mycobacterium tuberculosis H37Ra enzyme to apparent homogeneity.
abstract: 1. The enzyme (EC 2.7.1.63) was isolated from glucose-grown M. tuberculosis H37Ra; during the purification procedure, 2-mercaptoethanol, glucose, EDTA and NaCl served as protecting agents. 2. The enzyme was purified about 600-fold. The preparation was homogeneous on polyacrylamide-gel electrophoresis and gave one precipitin line in double immunodiffusion test. Molecular weight of the enzyme determined by Sephadex G-100 filtration was about 118 000. 3. The enzyme preparation showed also glucokinase activity with ATP.
mesh_terms: D002474:Cell-Free System; D005941:Glucokinase / Q000378:metabolism; D006358:Hot Temperature; D008970:Molecular Weight; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D010770:Phosphotransferases / Q000302:isolation & purification* / Q000378:metabolism; D013045:Species Specificity
chemical_list: D010770:Phosphotransferases; D005941:Glucokinase