Journal ArticleDOI
Acid Glycosidase Activities in the Cotyledons of Pisum sativum L.
Colette M. McGee,David R. Murray +1 more
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TLDR
The activities of α-mannosidase (isoenzyme 1) from pea cotyledons is inhibited by the indolizidine alkaloid swainsonine with an apparent K(i) of 1.37 \sx 10(-7) M.About:
This article is published in Journal of Plant Physiology.The article was published on 1984-11-01. It has received 5 citations till now. The article focuses on the topics: Sativum & Pisum.read more
Citations
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Journal ArticleDOI
Comparative Studies of Acid Glycosidases from Three Legumes
C. M. McGEE,D. R. Murray +1 more
Journal ArticleDOI
Localization of Acid Glycosidases in Protein Bodies of Pea Cotyledons
Colette M. McGee,David R. Murray +1 more
TL;DR: Protein bodies collected by centrifugation after cold water extraction of imbibed pea cotyledons were obtained in good yield and free of intact mitochondria, but they were practically devoid of α-mannosidase activity.
Journal ArticleDOI
Effects of cycloheximide and actinomycin D on glycosidase activities in the cotyledons of legume seeds following imbibition
TL;DR: It is concluded that acid glycosidase activities in imbibing cotyledons of these species generally result entirely from rehydration of enzyme molecules formed during seed development.
Journal ArticleDOI
Electrophoretic study of α-d-mannosidase and α-d-galactosidase from dry seeds of Pisum sativum
S Sklenářova,Marie Tichá +1 more
TL;DR: Affinity electrophoresis was used to study the interaction of the studied enzymes with saccharides; water-soluble O-glycosyl polyacrylamide copolymers and polysaccharides were used for the preparation of affinity gels.
Journal ArticleDOI
Purification of ±-Mannosidase from the Cotyledons of Pea Seeds (Pisum sativum L.)
TL;DR: The predominant swainsonine-sensitive form of α-mannosidase (EC 3.2.24) has been purified from the cotyledons of developing pea seeds by purification sequence involved extraction with Tris and substrate affinity could not be employed, because unlike the jack bean enzyme, the pea enzyme did not attach to yeast α- Mannan-Sepharose.
References
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Journal ArticleDOI
A Spectroscopic Investigation of Swainsonine: An α-Mannosidase Inhibitor Isolated from Swainsona canescens
TL;DR: In this article, a potent inhibitor of α-mannosidase was isolated from Swainsona canescens and was shown to be an indolizidinetriol by spectroscopic techniques and the relative stereochemistry was defined as 8aβ-indolizidine-lα,2α,8β-triol.
Journal ArticleDOI
Inhibition of lysosomal alpha-mannosidase by swainsonine, an indolizidine alkaloid isolated from Swainsona canescens.
TL;DR: Evidence is presented to suggest that swainsonine is a reversible active site-directed inhibitor of lysosomal alpha-mannosidase.
Journal ArticleDOI
Control of Storage Protein Metabolism in the Cotyledons of Germinating Mung Beans: Role of Endopeptidase
Maarten J. Chrispeels,D. Boulter +1 more
TL;DR: The results suggest that the appearance of a sulfhydryl-type endopeptidase activity is a necessary prerequisite for the rapid metabolism of the reserve proteins which accompanies germination.
Journal ArticleDOI
A storage role for albumins in pea cotyledons
TL;DR: Certain major polypeptides confined to the albumin fraction from the cotyledons were shown to be degraded in vivo following germination, thus functioning as a reserve of amino nitrogen and carbon skeletons.
Journal ArticleDOI
Changes in Activities of Enzymes of Nitrogen Metabolism in Seedcoats and Cotyledons during Embryo Development in Pea Seeds.
David R. Murray,Ivan R. Kennedy +1 more
TL;DR: The data indicate that the amide groups of imported asparagine and glutamine are metabolized differently, largely by asparaginase and glutamate synthase, respectively, and the central importance of alpha-ketoglutarate-glutamate cycling in the redistribution of amino groups associated with the net synthesis of amino acids and reserve proteins is emphasized.
Related Papers (5)
Arginine Catabolism in the Cotyledons of Developing and Germinating Pea Seeds
Hans de Ruiter,Chris Kollöffel +1 more