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. 1990 Apr 1;267(1):191–196. doi: 10.1042/bj2670191

Shedding of hyaluronate synthase from streptococci.

A Mausolf 1, J Jungmann 1, H Robenek 1, P Prehm 1
PMCID: PMC1131263  PMID: 2109602

Abstract

Hyaluronate synthase was shed into the culture medium from growing streptococci (group C) together with nascent hyaluronate. The mechanism of solubilization was analysed using isolated protoplast membranes. Solubilization increased when membranes were suspended in larger volumes, but it was temperature-independent and was not inhibited by protease inhibitors. Increased hyaluronate chain length enhanced solubilization. The soluble synthase could re-integrate into Streptococcal membranes in a saturable manner. The soluble synthase behaved like an integral membrane protein, although it was not integrated into phospholipid vesicles. In sucrose velocity centrifugation the synthase had a higher sedimentation rate in detergent-free solution, indicating that it existed in an aggregated state.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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