Isolation and characterization of prosthecae ofAsticcacaulis biprosthecum

Autor: T. L. Jordan, J. S. Porter, Jack L. Pate
Rok vydání: 1974
Předmět:
Zdroj: Archives of Microbiology. 96:1-16
ISSN: 1432-072X
0302-8933
Popis: Prosthecae were sheared from cells ofAsticcacaulis biprosthecum with a Sorvall omnimixer and purified by centrifugation. Removal of prosthecae resulted in no loss in viability. Purified prosthecae contain protein, carbohydrates and lipids. Certain enzymes that are present in the main body of the cell are also present in prosthecae: malic dehydrogenase (E.C. 1.1.1.37), alkaline phosphatase (E. C. 3.1.3.1), succinic dehydrogenase (E.C. 1.3.99.1), cytochromec reductase (E.C. 1.6.2.a), and cytochromes. Other enzymes present in whole cells are not in prosthecae: isocitric dehydrogenase (E.C. 1.1.1.41), NADH oxidase (E.C. 1.6.99.3), glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49), and lactic dehydrogenase (E.C. 1.1.2.3). Swarmer cells (non-prosthecate) were purified by allowing prosthecate cells to attach to cheesecloth in the growth medium. Envelopes prepared from prosthecae were compared with envelope from swarmer cells. The two envelope fractions differed in the disc-gel electrophoretic patterns of proteins solubilized from them.
Databáze: OpenAIRE