Trypsin solubilized hemagglutinin-neuraminidase of Sendai virus (cHN) displays michaelian kinetics, with native fetuin as substrate, at 37 degrees C. Vmax and Km values are only marginally altered, as compared to intact viral neuraminidase. At lower temperatures, cHN follows non-michaelian kinetics, with marked substrate inhibition at 4 degrees C. With denaturated fetuin, michaelian kinetics are observed in all conditions, while asialo fetuin was an uncompetitive inhibitor of cHN, with native fetuin or sialyl lactose as substrates. These results can be explained assuming that the protein moiety of fetuin acts as an allosteric inhibitor of cHN.

Allosteric inhibition of the water-soluble C-terminal fragment of Sendai virus neuraminidase / Dallocchio, F; Bellini, T; Martuscelli, G; Baiocchi, M; Tomasi, M. - In: BIOCHEMISTRY INTERNATIONAL. - ISSN 0158-5231. - 25:4(1991), p. 663-8.

Allosteric inhibition of the water-soluble C-terminal fragment of Sendai virus neuraminidase

Baiocchi, M;
1991

Abstract

Trypsin solubilized hemagglutinin-neuraminidase of Sendai virus (cHN) displays michaelian kinetics, with native fetuin as substrate, at 37 degrees C. Vmax and Km values are only marginally altered, as compared to intact viral neuraminidase. At lower temperatures, cHN follows non-michaelian kinetics, with marked substrate inhibition at 4 degrees C. With denaturated fetuin, michaelian kinetics are observed in all conditions, while asialo fetuin was an uncompetitive inhibitor of cHN, with native fetuin or sialyl lactose as substrates. These results can be explained assuming that the protein moiety of fetuin acts as an allosteric inhibitor of cHN.
1991
Allosteric Site; Kinetics; Neuraminidase; Parainfluenza Virus 1, Human; Peptide Fragments; Solubility; Substrate Specificity; Water; alpha-Fetoproteins
01 Pubblicazione su rivista::01a Articolo in rivista
Allosteric inhibition of the water-soluble C-terminal fragment of Sendai virus neuraminidase / Dallocchio, F; Bellini, T; Martuscelli, G; Baiocchi, M; Tomasi, M. - In: BIOCHEMISTRY INTERNATIONAL. - ISSN 0158-5231. - 25:4(1991), p. 663-8.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1221911
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