Isolation and characterization of multiple forms of papaya latex lysozyme
1995
Lakhtin, V.M. | Kostanova, E.A. | Arbatskij, N.P.
Ion-exchange chromatography and lectin chromatography were used to isolate from a lyophilized preparation of Carica papaya L. Latex electrophoretically (polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate) homogeneous forms of lysozyme that did or did not bind to lectin. The purified enzyme contains 4.1 mol. % of carbohydrates: glucose (83 %), galactose (9 %), xylose (4 %), mannose (3 %), N-acetylglucosamine (1 %) and fucose (trace amounts). The kinetic curves of splitting the micrococcal cells by the lysozyme preparations were biphasic: a phase of bacterial cell aggregation preceded the phase of disaggregation and lysis. The turbidimetric analysis of lysozyme activity, as indicated by the kinetics of hydrolysis of micrococcal cell walls, permitted the determination of lysozyme activity in the preparations of chitin-binding proteins and lectins
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