Occurrence of a large molecular size form of polyphosphate-glucose phosphotransferase in extracts of Mycobacterium tuberculosis H37Ra.
Extracts prepared by sonicating Mycobacterium tuberculosis H37Ra cells with subsequent centrifugation at 18,000 X g proved to contain a very large molecular size form of polyphosphate-glucose phosphotransferase. The enzyme was separable by polyacrylamide gel electrophoresis, DEAE-cellulose chromatography or ultracentrifugation. When rechromatographed at alkaline pH values, it gave rise to one of the soluble forms of lower molecular weight. The conversion also took place as a result of n-butanol extraction or salting out with ammonium sulfate and heating of dissolved pellet. Under certain conditions the lower-molecular weight enzyme converted to the higher-molecular weight form by association with a hitherto undefined cell constituent. It is assumed that both ionic and hydrophobic forces play a role in this interconversion phenomenon.
D002457:Cell Extracts / Q000032:analysis; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D008970:Molecular Weight; D009169:Mycobacterium tuberculosis / Q000166:cytology / Q000201:enzymology*; D010770:Phosphotransferases / Q000302:isolation & purification*; D014461:Ultracentrifugation / Q000379:methods
D002457:Cell Extracts; D010770:Phosphotransferases; C024812:polyphosphate-glucose phosphotransferase