Influence of pH on the formation of extracellular proteins by Staphylococcus aureus.
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Acid Phosphatase↗
Biomedical subjects
S Arvidson
Publications and source records attributed to S Arvidson.
Formation of bacteriolytic enzymes in batch and continuous culture of Staphylococcus aureus.
The formation of bacteriolytic enzymes of Staphylococcus aureus, with special reference to strain M18, was investigated under a variety of conditions. The bacteriolytic activity was tested by using whole cells of Micrococcus lysodeikticus as a substrate. Complex media were required for production, and a Casein Hydrolysate-Yeast Extract medium (CCY(I)) was superior to Brain Heart Infusion and Trypticase Soy Broth. The optimal pH level for production was 7.0. Effective oxygenation and exchange of the beta-glycerophosphate of the CCY(I) medium for glucose increased the rates of growth and autolysis and the rate of appearance of extracellular bacteriolytic enzymes. However, the extracellular lytic activity decreased more rapidly at the end of the growth period than under the standard culture conditions. The appearance of inhibitor(s), probably derived from autolysis, might be responsible for this rapid decrease. The highest yields were obtained in a continuous process in which the activity was almost twice that of batch cultures grown under the same conditions. The bacteriolytic activity produced in continuous culture had a considerably increased stability in the purification process. The advantage of producing unstable bacterial proteins in continuous culture under controlled growth conditions is discussed.
Bacteriolysis↗
The secretory S complex in Bacillus subtilis is identified as pyruvate dehydrogenase.
We have cloned the operon for the Bacillus subtilis S complex, which has been suggested to be a component of the protein secretion machinery. The S-complex operon was found to encode 4 proteins, which were identified as subunits of pyruvate dehydrogenase (PDH). The Staphylococcus aureus membrane-bound ribosome protein (MBRP) complex has been considered to be a counterpart of the B. subtilis S complex. Here, we sequenced a fragment of the MBRP operon encoding the C-terminal part of E1 beta, the entire E2 and the N-terminal part of the E3 subunit of PDH, thus conclusively confirming the PDH identity of the MBRP complex as well. It appeared unlikely that PDH could be a primary component in protein secretion, thus disproving the previous hypothesis of the role of the S complex. However, attachment of the S complex (PDH) to the membrane and ribosomes may produce a biologically significant interaction.
Bacillus subtilis↗
Intraocular levels of cefuroxime in inflamed rabbit eyes.
The pharmacokinetics of cefuroxime was studied in the inflamed rabbit eye employing subconjunctival, intravitreal and combined intravitreal-intravenous routes of administration to study the intraocular levels and the duration of minimum inhibitory concentrations (MIC) of the antibiotic in the vitreous and in the aqueous. A standard inoculum of viable S. aureus was injected into the vitreous of 36 pigmented rabbits to establish experimental endophthalmitis. A biological method was used for the antibiotic assay. Penetration of systemically and subconjunctivally administered-cefuroxime into the inflamed vitreous was poor. Intraocular inflammation increased the clearance of the intravitreally injected cefuroxime. A dose of 75 mg subconjunctivally produced levels in the aqueous far exceeding MIC for over six hours. Penetration of intravitreally injected cefuroxime into the aqueous was poor, inconsistent and short lasting. Following a single intravitreal injection of 1000 micrograms cefuroxime, levels exceeding the MIC for common ocular pathogens persisted in the vitreous for at least 24 hours but supplementation with intravenous cefuroxime neither increased the intraocular levels nor delayed the clearance of the intravitreally injected antibiotic.
Animals↗