Polyphosphate-glucose phosphotransferase. Purification of Mycobacterium tuberculosis H37Ra enzyme to apparent homogeneity
Szymona, M.; Kowalska, H.; Pastuszak, I.
Acta Biochimica Polonica 24(2): 133-142
1977
ISSN/ISBN: 0001-527X PMID: 406755 Document Number: 120141
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.