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- W2080454954 abstract "This paper describes a convenient procedure for the purification of fungal pectin transeliminase (PTE). Taking advantage of the enzyme's low isoelectric point (pH 3.5), a high degree of purification is obtained by column chromatography on DEAE cellulose. Additional steps in the procedure include passage through Sephadex G-75 and precipitation by dialysis against distilled water. The extraction of PTE from the acetone powder of pea seedlings is also described. Several properties of the purified enzyme were investigated. The enzymic reaction has an energy of activation of 8400 cal./mole. This may be compared to 23,000 cal./ mole for the inorganically catalyzed reaction. PTE is activated by multivalent anions and inhibited by multivalent cations. Plant hormones and their analogs inhibit the ability of PTE to attack pectin. This inhibition increases with increasing substrate (pectin) concentration. Pectin, partially degraded by heating at pH 6.8, is particularly effective. A number of substances have been compared in their ability to induce this inhibition. Different pectin samples exhibit a large variation in the degree to which they interact in this system." @default.
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- W2080454954 date "1962-04-01" @default.
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- W2080454954 title "Studies relating to the purification and properties of pectin transeliminase" @default.
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- W2080454954 doi "https://doi.org/10.1016/0003-9861(62)90050-4" @default.
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