FORMATION AND RELEASE OF HYALURONIDASE AND AMINOPEPTIDASE IN NON‐GROWING CELLS OF STREPTOCOCCUS MITIS, ATCC 903

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Abstract
Hyaluronidase synthesis in Streptococcus mitis (ATCC 903) was completely repressed during anaerobic growth in glucose‐containing media. A rapid synthesis of hyaluronidase was observed when exponentially growing, repressed cells were transferred to a proteose‐peptone medium lacking fermentable carbohydrates. The synthesis started after a lag of approximately 10 min and continued at a constant rate for about 20 min. Chloramphenicol completely inhibited the synthesis. The period of synthesis of hyaluronidase at maximal rate increased with increasing concentrations of proteose‐peptone, while the rate of synthesis was not accelerated by proteose‐peptone concentrations above 1 per cent. Aminopeptidase activity of the cells also increased in proteose‐peptone medium. This increase was not inhibited by chloramphenicol or by puromycin. The aminopeptidase activity of the cellsincreased with increasing concentrations of proteose‐peptone. The increase of both enzymes was most rapid at pH 7.4–7.7. The cells released hyaluronidase and aminopeptidase solely by autolysis. Autolysis in proteose‐peptone medium was most rapid at pH 7.4–7.7 and was not affected by variations in the proteose‐peptone concentration or by chloramphenicol.

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