Composition of Some Subcellular Fractions from Seeds of Arachis hypogaea<sup>a</sup>

Dieckert, Julius W.; Snowden, James E.; Moore, Anna T.; Heinzelman, D. C.; Altschul, Aaron M.

doi:10.1111/j.1365-2621.1962.tb00100.x

Cited by 71 publications

(28 citation statements)

References 20 publications

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“…This confirms the results of Dieckert et al (8) who found that the same proteins exist in different aleurone preparations separated by differential and density-gradient centrifugation. However, the presence of 1 antigen in the large aleurone fraction, which is not present in the small aleurone fraction could signify a' difference between these 2 particles or could simpfWi originate from contamination by the nuclei.…”

Section: Resultssupporting

confidence: 82%

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-Conarachin

1969

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Abstract. Fourteen antigenic constituents have been detected in A rachis hypogaea seeds. The major proteins of the classic arachin and conarachin fractions have been identified. Arachin contains 4 antigens (the major one called a-arachin) and conarachin contains 2 which have been called a,, and a2-conarachin. Structural differences between a-arachin, a1 and a2-conarachin are indioated by their different antigenic specificities. a-Arachin precipitates as a separate entity at low temperature. The action of trypsin on this protein induces an increase in electrophoretic mobility and prevents precipitation at low temperature. This enzyme has no detectable effect on a., and a,-conarachin.The proteins of the ootyledon and of the entire axis are quite similar in their immunoelectrophoretic patterns. However, quantitative and qualitative differences oocur between the proteins found in the cotyledon and those of the 1-millimeter tip of the axis. In the latter, there is a 4-fold smaller proportion of a-arachin than in the cotyledon. Immunoelectrophoretic analysis of subcellular preparations from cotytedons confirms that a-arachin is an aleurin and that c1-conarachin is a typical cytoplasmic protein. Large and small aleurone grains appear very similar in their qualitative antigenic composition.Proteins extracted from mature seeds of Arachis hypogaea appear heterogeneous by chromatography on DEAE-cellulose, ultracentrifugation and polvacrylamide gel electrophoresis (7, 10). Moreover, 2 of the reserve proteins, a-arachin and a-conarachin, associate or dissociate under different conditions of pH and ionic strength (17,18,19) to make the precise identification of individual components difficult or even uncertain. The fact that these 2 proteins exhibit similar electrophoretic mobilities (16) suggests structural similarities.Because of their high degree of specificity, immunological methods offer another approach for the study of peanut proteins. A general picture of the total proteins was established and the 2 major reserve proteins were characterized after submission to phys-

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Section: Resultssupporting

confidence: 82%

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-Conarachin

1969

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“…Therefore, it seems probable that the role of metalloproteinases is to initiate the enzymatic proteolysis of storage proteins. By contrast, in legume seeds where most protein bodies lack globoids (Pernollet 1978;Sobolev 1985) and the amount of phytin in these organelles in considerably lower (Dieckert et al 1962;Sobolev et al 1976), cysteine proteinases, synthesized de novo, appear to act as the starting enzymes for storage-protein proteolysis (Bewley and Black 1985;Shutov and Vaintraub 1987).…”

Section: Discussionmentioning

confidence: 99%

Localization of a metalloproteinase and its inhibitor in the protein bodies of buckwheat seeds

Elpidina

Voskoboynikova

Belozersky

et al. 1991

Planta

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Cotyledons of dry buckwheat (Fagopyrum esculentum Moench) seeds were used to study the cellular localization of a metalloproteinase which performs in vitro the initial limited proteolysis of the main storage protein of the seed, and of its proteinaceous inhibitor. Fractions of complex protein bodies (PB 1) and of the cytoplasm and membrane material (CMM) were obtained by fractionating cotyledons in a mixture of acetone and CCl4. The greater part of the metalloproteinase activity was found to be localized in the PB 1 fraction, with a lesser amount in the CMM fraction, whereas the metalloproteinase inhibitor was localized almost entirely in the PB 1 fraction. The data obtained indicate that the complex protein bodies of dry buckwheat seeds contain the components of the proteolytic system responsible for the initial degradation of the main storage protein - the 13S globulin - of buckwheat seeds, i.e. 13S globulin, the metalloproteinase, and its inhibitor. This confirms that it is possibile for the metalloproteinase to perform a controlled proteolysis of the 13S globulin in vivo. The effect of divalent cations on the degradation of the 13S globulin was also studied. A mechanism is discussed whereby the proteolysis of 13S globulin is initiated by divalent cations released as a result of phytin decationization during seedling growth.

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“…23 ) RNA was determined by the methods of Kirby24) and Dieckert et a1. 25 ) Lipid analysis. Lipids extracted from the subcellular fractions were analyzed by thin-layer chromatography.…”

Section: Methodsmentioning

confidence: 99%

Formation of Oleosomes in Maturing Safflower Seeds

Ichihara

1982

Agricultural and Biological Chemistry

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The accumulation of oil in maturing safflower seeds was studied with an electron microscope. It was suggested that net-like clusters of proteinaceous particles in the cytoplasm are the site of triacylglycerol synthesis. No evidence was obtained to support the hypothesis that oleosomes originate in the. endoplasmic reticulum. A hypothesis has been proposed that triacylglycerols are initially synthesized by the net-like clusters in the cytoplasm to form a protein-oil complex, and the triacylglycerols are concentrated in the center of the cluster as their formation proceeds.

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Composition of Some Subcellular Fractions from Seeds of Arachis hypogaea^a

Cited by 71 publications

References 20 publications

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-Conarachin

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-Conarachin

Localization of a metalloproteinase and its inhibitor in the protein bodies of buckwheat seeds

Formation of Oleosomes in Maturing Safflower Seeds

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Composition of Some Subcellular Fractions from Seeds of Arachis hypogaeaa

Cited by 71 publications

References 20 publications

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-Conarachin

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-Conarachin

Localization of a metalloproteinase and its inhibitor in the protein bodies of buckwheat seeds

Formation of Oleosomes in Maturing Safflower Seeds

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Product

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Composition of Some Subcellular Fractions from Seeds of Arachis hypogaea^a