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Infect Immun. 1979 December; 26(3): 879-882

Enzymatic induction of interferon production by galactose oxidase treatment of human lymphoid cells.

F Dianzani, T M Monahan, A Scupham and M Zucca

ABSTRACT

Human lymphocyte cultures produced large amounts of interferon after treatment with the enzyme galactose oxidase. Interferon production was detectable as early as 3 h after enzymatic treatment and reached a level of about 10(4) reference units 20 to 24 h later. Galactose oxidase-induced interferon appeared to be immune interferon on the basis of acid lability, lack of neutralization by antibody to leukocyte interferon, and slow kinetics of activation of the cellular antiviral state. Interferon production was inhibited to the same extent (99%) by pretreatment of the cells with beta-galactosidase or with neuraminidase followed by beta-galactosidase, suggesting that the critical event for activation of interferon production is the oxidation of exposed galactose residues on lymphocyte membrane.

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Infect Immun. 1979 December; 26(3): 879-882

This article has been cited by other articles:

• STIEHM, E. R., KRONENBERG, L. H., ROSENBLATT, H. M., BRYSON, Y., MERIGAN, T. C. (1982). Interferon: Immunobiology and Clinical Significance. ANN INTERN MED 96: 80-93 [Abstract]