The kappa and lambda antigens of <i>Clostridium welchii</i>

Oakley, C. L.; Warrack, G. Harriet; Warren, Marion E.

doi:10.1002/path.1700600317

Cited by 48 publications

(8 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Subsequent work at first seemed to indicate that essentially similar enzymes were produced by other organisms (23)(24)(25)(26)(27). However, it has been clearly established that other bacterial proteases exist, unable to attack "native" collagen, but more or less readily hydrolyzing collagen which has been "denatured" by various physical and chemical means (28)(29)(30)(31)22).…”

mentioning

confidence: 99%

Bacterial Digestion of Collagen 1

Maclennan¹,

Mandl²,

Howes³

1953

J. Clin. Invest.

View full text Add to dashboard Cite

mentioning

confidence: 99%

Bacterial Digestion of Collagen 1

Maclennan¹,

Mandl²,

Howes³

1953

J. Clin. Invest.

View full text Add to dashboard Cite

“…perfingens ClOSl formed a cell-bound azoreductase, but since assays of protease activity were carried out with cell-free culture supernatant fluids there was no effect on these measurements. Azocoll was used as general proteolytic substrate that could be hydrolysed by either kappa toxin (Kameyama & Akama 1971) or lambda toxin (Oakley et al 1948). No effort was made to differentiate the relative contributions to protein hydrolysis made by these enzymes.…”

Section: Resultsmentioning

confidence: 99%

Protease production by Clostridium perfringens in batch and continuous culture

Allison

Macfarlane

1989

Lett Appl Microbiol

View full text Add to dashboard Cite

1989. Protease production by Clostridium perfringens in batch and continuous culture. Letters in Applied Microbiology 9, 4-8.CIostridium perfringens C1051 isolated from human faeces was studied to determine physiological and nutritional factors that govern protease production in the colon. In batch culture extracellular protease was formed during exponential growth but ceased in the stationary phase. In both glucose-and peptide-limited chemostats protease activities increased with culture dilution rate. Proteolysis was greatest under glucose limitation at low growth rates (D = O.l/h to D = 0.35/h), but no difference was found in the relative amounts of protease produced when dilution rates were increased to 0.7/h. In batch culture protease formation was optimal at pH 6.0.Ammonium chloride and glucose concentrations over the range 1-10 g/l had no significant effect on protease production, but high concentrations of peptone were stimulatory.

show abstract

“…The toxins 6f C. perfringens are proteins. Many of them are also enzymes some of which are pioteolytic, including kappa toxin (collagenase) and lambda toxin (proteinase) (Oakley et al, 1948). Nekvasilova et al (1970) reported that a semi-synthetic medium, containing acid hydrolysate of casein supported growth without toxin production, whereas an enzymatic hydrolysate of casein supported growth and toxin synthesis.…”

Section: Resultsmentioning

confidence: 99%

Casein Inhibition of Clostridium perfringens Growth and Exoprotease Production

Curran

Solberg

Blaschek

et al. 1981

Journal of Food Science

View full text Add to dashboard Cite

Growth of C. perfringens strain 3624 on a defined medium containing ANRC Reference Casein as the nitrogen source was investigated. Gas production, monitored manometrically as an index of growth, indicated a depressed growth response of the organism in the casein‐containing medium. Increased growth response resulting from pepsin treatment of the casein was largely due to the enzyme serving as a nitrogen source. Chelation of iron by casein was not responsible for the growth inhibition. Casein suspended in complete medium was not inhibitory to the organism. Growth studies indicated that native casein was not available as a nitrogen source to the organism. Acid hydrolyzed casein and commercial casein hydrolysate served as suitable nitrogen sources for growth of the organism, however exoprotease production was repressed in both media as well as in medium containing native casein as the sole nitrogen source. C. perfringens strain 3624 produced exoprotease in the completely defined medium containing synthetic amino acids, indicating the possible presence of an amino acid or a metabolite, not produced in the casein‐containing medium which functioned to derepress the enzyme synthesizing mechanism.

show abstract

The kappa and lambda antigens of Clostridium welchii

Cited by 48 publications

References 5 publications

Bacterial Digestion of Collagen 1

Bacterial Digestion of Collagen 1

Protease production by Clostridium perfringens in batch and continuous culture

Casein Inhibition of Clostridium perfringens Growth and Exoprotease Production

Contact Info

Product

Resources

About