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PMID: 16661165 Published · ppublish English Journal Article

Presence in Dry Pea Cotyledons of Soluble Succinate Dehydrogenase That Is Assembled into the Mitochondrial Inner Membrane during Seed Imbibition.

Plant physiology ·Vol. 65 ·No. 2 ·1980-02-00 ·Pages 229-33

Nakayama N, Sugimoto I, Asahi T

Abstract

SUCCINATE DEHYDROGENASE (SUCCINATE: phenazine methosulfate oxidoreductase, EC 1.3.99.1) activity in crude mitochondrial fraction from pea (var. Alaska) cotyledons increased during seed imbibition to reach a maximum after about 12 hours. The increase was not inhibited by either cycloheximide or d(-)threo-chloramphenicol. The postmicrosomal fraction from dry cotyledons, but not that from fully imbibed ones, contained a soluble form of succinate dehydrogenase. The soluble enzyme was partially purified by ammonium sulfate fractionation and diethylaminoethyl-cellulose and Sepharose 6B column chromatography. The enzyme showed no succinate-coenzyme Q oxidoreductase activity and had a molecular mass of about 100,000 daltons. The soluble enzyme seemed to differ only slightly from succinate dehydrogenase solubilized from the mitochondrial inner membrane from fully imbibed cotyledons by a detergent. It is proposed that the soluble succinate dehydrogenase is associated with an inert mitochondrial inner membrane in dry cotyledons to form an active one during seed imbibition.

Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Nakayama N
Laboratory of Biochemistry, Faculty of Agriculture, Nagoya University, Chikusa, Nagoya 464, Japan.
Sugimoto I
Asahi T
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16 references, click to expand
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Article Info
Journal
Plant physiology
Abbr.
Plant Physiol
ISSN
0032-0889
DOI
10.1104/pp.65.2.229
Published
1980-02-00
Pages
229-33
Language
English
Region
United States
NLM ID
0401224
PMCID
PMC440302
External Links
PubMed source DOI: 10.1104/pp.65.2.229 PMC Full Text View journal details
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