Abstract
The relative rates of catabolism of glucose and glucose-6-phosphate by intact-cell suspensions of the meningopneumonitis agent, a member of the psittacosis group (Chlamydia), and the properties of the hexokinase and glucose-6-phosphate dehydrogenase of these suspensions were investigated. It is proposed that the hexokinase is a host enzyme bound to the surface of the meningopneumonitis cell and that glucose-6-phosphate is the first substrate in the conversion of hexose to pentose to be attacked by enzymes synthesized by the meningopneumonitis agent.
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Selected References
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