Fructose 1,6-bisphosphate aldolases from vegetative cells and spores of some bacilli

• Published in: Journal of biochemistry (Tokyo) 1978-02, Vol.83 (2), p.503-510
• Main Authors: UJITA, Susumu, SHIROZA, Teruaki, KIMURA, Kinuko
• Format: Article
• Language: English
• Subjects: Bacillus - enzymology; Calcium - pharmacology; Chloromercuribenzoates - pharmacology; Edetic Acid - pharmacology; Fructose-Bisphosphate Aldolase - isolation & purification; Fructose-Bisphosphate Aldolase - metabolism; Molecular Weight; Picolinic Acids - pharmacology; Spores, Bacterial - enzymology; Temperature
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a131937

Vegetative cell and spore fructose 1,6-bisphosphate aldolases [EC 4.1.2.13] were partially purified from Bacillus subtilis168, Bacillus licheniformis and Bacillus cereus IFO 3466, and their properties were compared with those of the aldolases previously purified from Bacillus subtilis PCI 219. The molecular weights of aldolases from B. subtilis 168 and B. licheniformis were similar to those of the aldolases from B. subtilis PCI 219 and were found to be 150,000±20,000 by gel filtration, but the molecular weights of B. cereus aldolases were smaller than those of B. subtilis PCI 219 aldolases, being 60,000±3,000. However, no differences between the vegetative cell aldolase and the spore aldolases were detected even in the case of B. cereus IFO 3466. On the other hand, the subunit sizes of their aldolases were estimated by SDS-gel electrophoresis and all of the subunit sizes of vegetative cell and spore aldolases from the bacilli were found to be similar, 30,000±2,000. Differences between the aldolases of B. subtilis PCI 219 and B. cereus IFO 3466 were found in electrophoretic mobilities, but all of the aldolases resembled each other in such properties as the inhibition by metal chelators and a sulfhydrul reagent. No differences between vegetative cell and spore aldolases from each bacilli were observed except for the thermal stability of B. cereus IFO 3466 aldolases. The molecular weights of aldolases from B. subtilis PCI 219 and B. cereus IFO 3466 in the presence of substrate were also estimated by means of sucrose density gradient centrifugation. The molecular weight of each aldolase did not change; the same values as in the absence of substrate were obtained.