Abstract
Several purification methods were tested and the optimal procedure for obtaining L-lysine α-oxidase from fungiTrichoderma sp. and its isoform (minor L-lysine α-oxidase) was worked out. The enzyme and its isoform were obtained in a homogeneous state, the most important physicochemical properties were studied, and a number of differences between them were found. The most marked differences between L-lysine α-oxidase and its isoform were observed in the molecular weight (120 and 100 kD, respectively), in the isoelectric point (pI 4.4 and 5.6, respectively), and in the specific activity (90–95 and 17–20 U/mg) in experiments where L-lysine where used as substrate.
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Translated fromByulleten' Eksperimental'noi Biologii i Meditsiny, Vol. 121, No. 4, pp. 404–406, April, 1996
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Vesa, V.S., Lukasheva, E.V., Khaduev, S.K. et al. Isoforms of L-lysine α-oxidase fromTrichoderma sp. . Bull Exp Biol Med 121, 368–370 (1996). https://doi.org/10.1007/BF02446729
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DOI: https://doi.org/10.1007/BF02446729