α-Conarachin

Dechary, J. M.; Talluto, Katherine F.; Evans, William J.; Carney, William B.; Altschul, Aaron M.

doi:10.1038/1901125b0

Cited by 54 publications

(32 citation statements)

References 6 publications

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“…Semiquantitative evxaluations showed that a1-conarachin and a-arachin disappear during germination, confirming results of Dechary et al (4). The disappearance of a2-conarachin was not as obvious, hence, a2-conarachin cannot be considered a reserve protein in the category of a1-conarachin and at-arachin.…”

Section: Discussionsupporting

confidence: 77%

“…, of extracts of roots removed 5 days after the beginning of germination (2 and 3) is shown using the corresponding antiroot immune serum (trough below 1) and using this serum previously absorbed with the cotyledonary extract of mature seeds (trough below 3). Wells in (4) were filled after electrophoresis with different quantities of the cotyledonary extract of mature seeds to check the absorption technique. IEA using the preceding absorbed immune sera of extracts of roots removed 2 days (5), 5 days (6), 9 days (7), and 14 days (8) …”

Section: Methodsmentioning

confidence: 99%

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Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. II. Protein Modification During Germination

1969

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Abstract. a-Conarachin and a-arachin are metabolized differently during germination.The amount of a-conarachin decreases without the appearance of antigenic intermediary compounds. a-Arachin retains its original antigenic structure and beoomes more anodic during germination, but a number of intermediary proteins, differing widely in electrophoretic mobility, form up to 14 days germination. The electrophoretic shift of a-arachin, detectable after 1 day of germination, might be caused by progressive deamidation of glutamine and asparagine. Decreases in amide content of protein extracted after germination support the hypothesis and suggest that a-arachin provides the first source of ammonia to the new seedling.New antigenic proteins are synthesized in both roots and cotyledons during germination. Some appear organ specific, whereas others are identical in both the cotyledons and the roots. Appearance and disappearance of each new protein is unique with respect to period of germination and hence might correspond to specific events of germination.It is generally assumied that the reserve proteinis of the seed are hydrolyzed during germiiniationi providing amlino acids for the synthesis of niew proteins (2). a-Arachin and a-colnarachin, the major reserve proteins of classic arachinl and conarachin in A4rachis hypoga,ea, progressively decrease during germination (4). They are located in different subcellular fractions and have different characteristics (3). This suggests different metabolic functions and modifications during germination. The aim of this study was to follow the fate of these proteins during germination. The results suggest a particular metabolic role for a-arachin. Materials and MethodsGermtinatioz. Seeds of Arachis hypogaea were germinated in vermiculite at 220 in lots of 20, eaclh seed weighing 1 ± 0.1 g. Sample lots were withdrawn at 2, 5, 8, 9, and 14 days of germlinationl. Germination was performed in the light.Extraction. Twenty cotvledons from each germlinated sample were extracted with 60 ml of buffer; 2 g of roots were extracted with 10 ml of buffer as described previously, (3). Immntunochemnical Methods. Double diffusion according to Ouchterlony (12), immunoelectrophoretic

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Section: Discussionsupporting

confidence: 77%

Section: Methodsmentioning

confidence: 99%

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. II. Protein Modification During Germination

1969

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“…The evidence presented here suggests that a-conarachin exists in approximately equal quantities in both subcellular fractions isolated. Dechary et al (6) showed that a-conarachin disappears almost entirely after 3 days of germination. The work of Daussant et (Figs.…”

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confidence: 99%

“…Since aleurone grains are sedimented at 10,000g, this suggests that the proteins in the fines fraction represent primarily cytoplasmic and microsomal components which are not associated with particles the size and density of aleurone grains. From the classification of Dechary et al (6) mobilities with ultracentrifuge sedimentation data can be of considerable interest in structural studies. Other factors, such as adsorbed ions, can also affect the associated state of parent species, inducing changes in mobility and sedimentation.…”

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Physicochemical Studies on the Proteins of the Peanut Cotyledon and Embryonic Axis

Neucere¹,

Ory²

1970

Plant Physiol.

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Subcellular fractions fronm the cotyledon obtained bv differential aind density gradient centrifugation, and extracts of total proteins from botlh cotyledon and axial tissues were analyzed by diethvlaminoethyl cellulose clironiatography, zone electrophoresis, ultracentrifugatioti, immunodiffusion, and immunoelectrophoresis. Fractionation and characterization of proteinis in subcellular organelles of the peanut reaffirin that a-arachin is located in the protein bodies of the cells. Results obtained bv diethlv-laminoetlhyl cellulose chromatograplhy of subeelltular fractions suggest that soine of the conaraclhin proteins are cytoplasmic. am-Conarachin is cv toplasmic, and a2-conarachin is particle-botund. a-Arachiii and a2-conarachin predonminate in the cotyledon. Quantitative differences for other proteins were also observed. Althlotuglh qualitative similarities are apparent by iimuiitnoelectroplhoresis, nmajor differences were observed in tde sedimiientation patterns, zone electroplioreograms, antd ill the dietlhvlaminoethvl cellulose chromatograms of total proteini extracts fromn the cotyledon and the axis.The major proteins of the peanut cotyledon have been characterized as albumins and globulins. The globulins, considered primarily as the reserve or storage proteins of the seed, were first classified by Johns and Jones (10) and by Jones and Horn (14) according to their solubility in ammonium sulfate. The two classic globulin fractions, arachin and conarachin, have been studied extensively by several investigators (4, 5, 11-13). They exist as complex systems with sedimentation and electrophoretic patterns which change considerably, depending upon the experimental conditions employed. The major proteins of classic arachin and conarachin have been named a-arachin and a-conarachin. Although homogenous by zone electrophoresis and sedimentation analysis, immunoelectrophoresis has shown that arachin contains four proteins (a-arachin being the major component) and a-conarachin contains two components called al-and a2-conarachin (5, 6). Preparation of Protein Extracts. Two grams of each tissue were homogenized in a Sorvall Omni-Mixer' in 8 ml of phosphate buffer, pH 7.9, ionic strength 0.2 (0.008 M NaH2PO4 -H20 0.64 M Na2HPO4) at 5 C. The homogenate was strained through four layers of cheesecloth, and the filtrate was clarified by centrifugation at 37,000g for 30 min in a Sorvall RC-2 centrifuge at 20 C. The final supernatant was dialyzed against phosphate buffer, pH 7.9, ionic strength 0.03 for 24 hr at 5 C. After warming to room temperature (25 C), the extracts were recentrifuged at 37,000g for 30 min to yield slightly turbid supernatants. These extracts and those from subcellular fractions were employed in the following investigations.

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Pflanzliche Samenglobuline als dissoziierende und assoziierende Proteinsysteme

Schwenke¹

1975

Nahrung

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α-Conarachin

Cited by 54 publications

References 6 publications

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. II. Protein Modification During Germination

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. II. Protein Modification During Germination

Physicochemical Studies on the Proteins of the Peanut Cotyledon and Embryonic Axis

Pflanzliche Samenglobuline als dissoziierende und assoziierende Proteinsysteme

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