Abstract
Studies on the Enzymatic Equipment of Erysipelothrix Hyaluronidase was detected in Erysipelothrix and discussed as a spreading factor some years ago [1]. Our latest investigations revealed the existence of aminopeptidases specific against L-lysine, L-arginine, L-alanine, L-leucine, L-isoleucine, L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine. Furthermore, a chymotrypsine-like enzyme splits N-benzoyl-DL-phenylalanine-2-naphthylamide, whereas N-(3-carboxypropionyl)-phenylalanine-p-nitroanilide is not split. The pathogenic role of these enzymes has been unclear up to now. There is, however, some evidence of a damaging action in the infected host (Müller, in preparation). Our studies concentrated on neuraminidase [2, 3]. This enzyme is found in many pathogenic but only in a few apathogenic bacteria, as shown in Table 1.
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References
Benco V, Brundjak Z (1953) Hyaluronidase bei Rotlaufbakterien. Vet Arch 23:283
Müller HE (1974) Die pathogenetische Bedeutung mikrobieller Neuraminidasen. Dtsch Med Wochenschr 99:1933
Müller HE (1974) Neuraminidases of bacteria and protozoa and their pathogenetic role. Behring Inst Mitt 55:34
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© 1981 Springer-Verlag Berlin Heidelberg
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Müller, H.E. (1981). Neuraminidase and Other Enzymes of Erysipelothrix rhusiopathiae as Possible Pathogenic Factors. In: Deicher, H., Schulz, LC. (eds) Arthritis. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68106-6_7
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DOI: https://doi.org/10.1007/978-3-642-68106-6_7
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-10781-1
Online ISBN: 978-3-642-68106-6
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