Intracellular distribution of seed proteins

Altschul, Aaron M.; Snowden, James E.; Manchon, Delphine; Dechary, J. M.

doi:10.1016/0003-9861(61)90166-7

Cited by 23 publications

(9 citation statements)

References 2 publications

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“…The subcellular distribution of a-arachin and a-conarachin confirm by different methods the conclusions of Altschul et al (2,3) that a-arachin is an aleurin. Moreover our results suggest that both small and large aleurone grains contain a-arachin.…”

Section: Resultssupporting

confidence: 73%

“…A general picture of the total proteins was established and the 2 major reserve proteins were characterized after submission to phys- 1 Presented in part at the 154th National American Chemical Society Meeting, Chicago, Illinois, 1967, by N. J. Neucere. 2 Present address: Service de Chimie Microbienne, Institut Pasteur, Paris 15e, France. 3 Present address: Oilseed Crops Laboratory, SURDD.…”

mentioning

confidence: 99%

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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: 73%

mentioning

confidence: 99%

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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“…These structures are easily isolated as a pellet following centrifugation of a pea cotyledon homogenate. The presence of similar protein bodies in peanut cotyledons has already been reported (1,3).…”

Section: Introductionsupporting

confidence: 59%

Intracellular Distribution of Proteins in Pea Cotyledons

Varner¹,

Schidlovsky²

1963

Plant Physiol.

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IntroductionAs a part of a study of organ and cellular senescence in plants, wve are delineating the structural and functional changes which occur in the cotyledons of germinating peas. As might have been expected from earlier reports that cotyledon cells are capable of performing oxidative phosphorylation, incorporation of labeled amino acids into protein (4) and de novo synthesis of certain enzymes (5), examination by electron microscopy showed the presence of all structures normally present in plant cells. In addition, a major fraction of the cell volume was found to be occupied with relatively large roughly spherical bodies, with no visible internal structure. The data presented here indicate that the reserve globulins are localized in these structures. These structures are easily isolated as a pellet following centrifugation of a pea cotyledon homogenate. The presence of similar protein bodies in peanut cotyledons has already been reported (1, 3). Material & MethodsThe peas (Pisunt sativurn, var. Early Alaska) were soaked in 1 % sodium hypochlorite for 30 minutes, rinsed in sterile distilled water, and transferred to moist sand in sterile Petri dishes. After one to three days' incubation at 25 C. the cotyledons were excised and examined microscopically and chemically. For Figure 5, 6, and 7 show the results of the chromatography of the various fractions OI1 DEAE colunmns and further support the conclusion that tile iiain component of the pellet and the proteiin bodlies is the globulin fraction and that the globulin fractioll is the major protein fraction of the pea cotyledon cells. It is interesting to note that the chromiiatograpllic separationl suggests the presence of four comiiponents in the globulin fraction while ultracentrifugal analyses indicate tw o major components (2).The supernatant fraction chromatographe(l in figure 8 -as from cotyledons of 3-daV old germlinating peas. The first pyrophosphatase peak may be an artifact. The three nmajor peaks always appear during cliromiiatography and the last pyrophosp)llatase peak increases greatly (luring tile third to sixtlh lays of germination. The sniall adenosine triphosphatase peak results froill the low activity of tile corresponding pyrophosphatase peak toward ATI at pH 7.1. The major adenosine triphosphatase peatk increases greatly duriing germiiiatioll an(l is the einzvnme stu(lied earlier by Young ail(l Varner (5). Tile proteins which becomle labeled in vivo fr-omii C14-labeled amiinio aci(ds (4) are in tile albulliin fraction and separate into five or six (liscrete peaks under the chromatographic con(litiolns use( hlere. B' a COIllbinlation of ill Xvixo iiltro(luctioil of lalbeledl aniiiio acids into proteills and the separation of these proteills by column cllromatographyv we liope to be able to identifv those enzymes which increase ill activity as a result of (le ilovo syntiesis and those whici illcrease as a result of solle kinld of activation. SummaryElectronmllicrograplis of pea cotyledon cells show that roughly-spherical bodies of about t...

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“…These were American No. 2 grade commercial samples, which were dehulled and hexane extracted, milled, and the material passing a 350 mesh sieve used. Some Nigerian bean-were also used; these were an ordinary commercial sample.…”

Section: Methodsmentioning

confidence: 99%