Definitions of antibodies to the antitumor enzyme L-lysine-α-oxidase, the study of its immunogenic properties and allergenic activity

Authors

  • I.P. Smirnova Peoples’ Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, Moscow, 117198, Russian Federation
  • V. Podoprigora Peoples’ Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, Moscow, 117198, Russian Federation
  • V.I. Kuznetsov Peoples’ Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, Moscow, 117198, Russian Federation
  • T.I. Mansur Peoples’ Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, Moscow, 117198, Russian Federation
  • I.G Bashkirova Peoples’ Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, Moscow, 117198, Russian Federation
  • M.S. Das Peoples’ Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, Moscow, 117198, Russian Federation

Keywords:

The antitumor enzyme, L-lysine-α-oxidase, Trichoderma

Abstract

The determination of antibodies to the antitumor enzyme L-lysine-α-oxidase Trichoderma harzianum Rifai F-180 was studied using enzyme-linked immunosorbent assay. It was shown that when testing the enzyme in mice and guinea pigs at a dose of 35 U / kg, the antitumor enzyme L-lysine-α-oxidase has low immunogenicity. Antibodies not only reduce catalytic activity, but also affect the affinity of the enzyme with the substrate. Guinea pigs showed that native and modified L-lysine-α-oxidase at a dose of 35 U / kg in vivo and in vitro has a weak allergenic activity.

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