Purification of Hyaluronidase from Clostridium perfringens

Baker, Eugene M.; Webster, Marion E.; Freeman, Monroe E.; Cary, Sylvia G.; Sanders, Arvey C

doi:10.3181/00379727-91-22158

Cited by 17 publications

(4 citation statements)

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“…Brunish and Mozersky (5) reported a 132-fold increase in specific activity of hyaluronidase from Escherichia freundii when extracts were chromatographed on IRC-50 cation exchange resin. Baker et al (3) purified Clostridium perfringens hyaluronidase 1,000-fold by using ammonium sulfate fractionation followed by three ethyl alcohol fractionations at pH 9.0, 6.8, and 7.5, respectively. Streptococcal hyaluronidase has been purified by ammonium sulfate fractionation followed by treatment with cholesterol (22).…”

Section: Discussionmentioning

confidence: 99%

Staphylococcal Hyaluronate Lyase: Purification and Characterization Studies

Abramson

Friedman

1968

J Bacteriol

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Staphylococcal hyaluronate lyase (hyaluronidase) derived from a pathogenic strain of staphylococcus was purified by means of salt fractionation with ammonium sulfate and gel filtration through Sephadex G-100. Most of the enzyme activity from concentrated culture supernatant fluids of staphylococci was obtained in a fraction precipitated by 90 to 100% saturation with ammonium sulfate. A small amount of enzyme was also precipitated by 80 to 90% saturation with the salt. The hyaluronidase-rich fractions did not contain other staphylococcal enzymes, such as coagulase, protease, lipase, and staphylokinase. These enzymes were present in the original concentrates. Molecular sieving chromatography of the partially purified enzyme by filtration through Sephadex G-100 resulted in a further increase in specific enzyme activity. However, more than one active peak was obtained after gel filtration, thus suggesting that there may be more than one molecular form of the enzyme. Immunodiffusion in agar gel of the chromatographically purified enzyme fraction, with immune serum from rabbits injected with concentrated staphylococcal culture supernatant fluids, indicated that there was one major antigen. A similar antigen, giving reactions of identity with the purified material, was present in the original culture supernatant fluid.

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Section: Discussionmentioning

confidence: 99%

Staphylococcal Hyaluronate Lyase: Purification and Characterization Studies

Abramson

Friedman

1968

J Bacteriol

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“…The μ-toxin is a minor toxin that has been implicated in the onset and progression of gas gangrene due to its ability to degrade hyaluronan, 10 an important constituent of connective tissue comprising linked glucuronic acid and N-acetyl glucosamine moieties. Encoded by the nagH gene, 11 the μ-toxin enhances the ability of C. perfringens and α-toxin to propagate through the infected tissue.…”

Section: Introductionmentioning

confidence: 99%

The Solution Structure of the C-terminal Modular Pair from Clostridium perfringens μ-Toxin Reveals a Noncellulosomal Dockerin Module

Chitayat¹,

Adams²,

Furness³

et al. 2008

Journal of Molecular Biology

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“…Clostridium perfringens, a common source of food poisoning as well as the causative agent of myonecrosis or gas gangrene (McDonel 1986;Rood and Cole 1991), has long been listed among the active producers of bacterial hyaluronidase (EC 4.2.2.1 hyaluronate lyase). Its cultivation products have been used for the isolation and/or characterization of this enzyme (Robertson et al 1940;Byers et al 1949;Becker et al 1956;Ispolatovskaya 1970, 1973;Canard et al 1994). Moreover, for several years Cl.…”

Section: Introductionmentioning

confidence: 99%

“…1940 ; Byers et al . 1949 ; Becker et al . 1956 ; Klimacheva & Ispolatovskaya 1970, 1973; Canard et al .…”

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Acceleration of hyaluronidase production in the course of batch cultivation of Clostridium perfringens can be achieved with bacteriolytic enzymes

Žukaitė¹,

Biziulevičius²

2000

Lett Appl Microbiol

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As Clostridium perfringens hyaluronidase has cell‐bound enzyme features, an enzymatic approach has been designed to facilitate the release of hyaluronidase into culture through increasing the clostridial cell wall permeability. As a result of the application of lytic peptidase from Actinomyces rutgersensis,β‐N‐acetylglucosaminidase and β‐N‐acetylmuramidase (both from Bacillus subtilis) commercially available preparations at the end of the producer's exponential growth phase, a 5·3‐, 4·8‐ and 4·0‐fold acceleration, respectively (but no enhancement), of hyaluronidase production in the course of batch cultivation of Cl. perfringens has been achieved. This also resulted in an approximately 10‐fold reduction in undesirable side lecithinase activity irrespective of the bacteriolytic enzyme preparation used.

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Purification of Hyaluronidase from Clostridium perfringens

Abstract: Renal inflammation tended to persist after ease and hypertension did not develop; however. the lesions were Of insufficient severity to produce azotemia. scopic findings.

Cited by 17 publications

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Staphylococcal Hyaluronate Lyase: Purification and Characterization Studies

Staphylococcal Hyaluronate Lyase: Purification and Characterization Studies

The Solution Structure of the C-terminal Modular Pair from Clostridium perfringens μ-Toxin Reveals a Noncellulosomal Dockerin Module

Acceleration of hyaluronidase production in the course of batch cultivation of Clostridium perfringens can be achieved with bacteriolytic enzymes

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