Neuraminidase Activity in Mycoplasma gallisepticum

Author:

Sethi K. K.1,Müller H. E.1

Affiliation:

1. Institut für Medizinische Mikrobiologie und Immunologie der Universität Bonn, 53 Bonn-Venusberg, West Germany

Abstract

The whole viable Mycoplasma gallisepticum (strain TT) organisms were found to possess neuraminidase activity with a p H optimum of 5.8 on substrates such as human transferrin, human α 1 -glycoprotein, and rabbit serum. The enzyme operated optimally at p H 4.5 when N -acetylneuraminyl-lactose was used as the test substrate.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference10 articles.

1. Sialic acid binding sites: role in haemagglutination by Mycoplasma gallisepticum;Gesner B.;Science,1965

2. Hayflick L. 1967. Tissue cultures and mycoplasmas. Tex. Rep. Biol. Med. 23:(Suppl. 1)285-303.

3. Neuramidase and neuraminidase-labile substrates in experimental influenza virus encephalitis;Kelly R. T.;Biochim. Biophys. Acta,1965

4. The determination of enzyme dissociation constants;Lineweaver H.;J. Amer. Chem. Soc.,1935

5. Haemadsorption and haemagglutination by mycoplasmas;Manchee R. J.;J. Gen. Microbiol.,1965

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