Abstract
Abstract A 400-fold purification of two isoenzymes of acid invertase (pH optima 4.5) and a two- to three-fold purification of alkaline (pH optima 7.5) invertase from suspension cultured carrot cells was obtained using ion-exchange (DEAE cellulose) and affinity (concanavalin-A) column chromatography. SDS polyacrylamide gel electrophoresis resolved major polypeptide bands at 61 000 and 49000 corresponding to the two isoenzymes of acid invertase, designated acid- 1 and acid-2, respectively. The acid invertase isoenzymes, in contrast with alkaline invertase, are likely glycoproteins based on their ability to bind the lectin concanavalin-A.
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