Reactivation by a bacterial acetate: Enzyme ligase of plant glyoxysomal isocitrate lyase

Geissler, Wolfgang G.; Kindl, Helmut

doi:10.1016/0014-5793(75)80289-4

Cited by 5 publications

(1 citation statement)

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“…Together with our recent studies on malate synthase, citrate synthase, malate dehydrogenase [13], thiolase, crotonase, 3-hydroxyacyl-CoA dehydrogenase [25], catalase [8] and earlier investigation on isocitrate lyase [26], this report complements our knowledge of microbody proteins.…”

Section: Discussionsupporting

confidence: 73%

Plant Microbody Proteins

Frevert

Kindl

1978

European Journal of Biochemistry

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Isocitrate lyase from cotyledons of cucumber seedlings (Cucumis sativus) has been purified 100‐fold. Two methods of preparing the soluble glyoxylate cycle enzyme are described: an elaborated method which used crude extracts of cucumber cotyledons, and another procedure which started with purified glyoxysomes from 4‐day‐old cotyledons and included a separation of glyoxysomal matrix enzymes by zonal centrifugation. The product behaved as a single species when tested by (a) polyacrylamide gel electrophoresis in the presence of dodecyl sulfate, (b) zonal centrifugation, and (c) double immunodiffusion against rabbit antibody to isocitrate lyase. Isocitrate lyase of cucumber glyoxysomes exhibited a molecular weight of 255 000 and was composed of four apparently identical subunits of Mr 64 000. An isoelectric point of 5.9 was determined. It was shown that isocitrate lyase is a glycoprotein, (a) by Schiff stain on polyacrylamide gels, (b) by periodate oxidation of the enzyme, subsequent reduction with NaB[3H]4 and electrophoretic analysis of the labelled glycoprotein, and (c) by incorporation of [3H]glucosamine in vivo into a protein which could be precipitated with antibodies to isocitrate lyase and revealed a 64 000‐Mr band upon electrophresis.

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Section: Discussionsupporting

confidence: 73%