A COMPARISON OF SOME PROPERTIES OF VICILIN AND LEGUMIN ISOLATED FROM SEEDS OF <i>PISUM SATIVUM, VICIA FABA</i> AND <i>CICER ARIETINUM</i>

Jackson, Phil; Boulter, D.; Thurman, David A.

doi:10.1111/j.1469-8137.1969.tb06416.x

Cited by 77 publications

(26 citation statements)

References 9 publications

(12 reference statements)

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“…Despite the considerable variation in subunit patterns exhibited by the legumin variants (see below) they all possessed only the three N-terminal groups (leucine, threonine and glycine) previously observed for Pisum sativum (Jackson et at., 1969) and Vicia faba (Wright and Boulter, 1974) legumin. In every case the relative intensities of dansyl-end-groups were leucine > glycine > threonine and in one case (JI 849) dansyl-threonine was barely discernible.…”

Section: Results (I) Variation In Leguminmentioning

confidence: 99%

Genetic variability in the structure of the α-subunits of legumin from Pisum—a two-dimensional gel electrophoresis study

Casey

1979

Heredity

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SUMMARYVariant forms of legumin (one of the major storage globulins of Pisum seeds) were purified by immunoaffinity chromatography from a range of Pisum types, includingP.fulvum, and primitiveforms, modern cultivars and advanced breeding selections of P. sativuin. The purified variants, all of which had sedimentation coefficients of about 12S and leucine, threonine and glycine as N-terminal amino acids, showed subunit heterogeneity on polyacrylamide gels containing sodium dodecyl sulphate and on two-dimensional isofocusing/electrophoresis. Comparison of legumins from different Pisum types showed variability, both in the net surface charge of the whole molecule and in the nature of subunit heterogeneity on two-dimensional gels. The usefulness of two-dimensional gels in the genetic analysis of pea seed storage protein structure was stressed and the role of potential artefacts in such analyses assessed.

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Section: Results (I) Variation In Leguminmentioning

confidence: 99%

Genetic variability in the structure of the α-subunits of legumin from Pisum—a two-dimensional gel electrophoresis study

Casey

1979

Heredity

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“…O predomínio da fração globulina tem despertado crescente interesse pelo isolamento e caracterização dessa fração em diferentes gêneros e espécies, destacando-se Vicia faba [40], Pisum sativum [19], Glycine max [21] e Phaseolus [8,38], entre outros [13]. Característi-cas distintas de solubilidade em sal, coeficiente de sedimentação em ultracentrífuga e peso molecular tem revelado a presença de duas frações globulínicas majoritárias, onde na grande maioria dos gêneros parece predominar a fração 11S (tipo legumina), enquanto no Phaseolus a 7S (tipo vicilina) é a fração principal [13].…”

Section: -Introduçãounclassified

Caracterização e hidrólise in vitro da globulina principal de grão-de-bico (Cicer arietinum L.), var. IAC-Marrocos

Neves¹,

Silva²,

Lourenço³

2004

Ciênc. Tecnol. Aliment.

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RESUMONo presente estudo procedeu-se ao isolamento e caracterização da fração globulina majoritária (11 S) de grão-de-bico, var. IACMarrocos. A globulina majoritária extraída foi isolada por cromatografia de filtração em gel e de troca-iônica mostrando apenas uma banda de proteína na eletroforese em gel de poliacrilamida. A globulina majoritária, após passagem em coluna de Sephadex, revelou duas bandas protéicas de 55 e 52,5kDa e três bandas menores em gel de poliacrilamida dodecilsulfato de sódio. Na presença de 2-mercaptoetanol 6 polipeptídios na faixa de 18 a 42kDa foram revelados na eletroforese. A globulina isolada foi submetida à ação da tripsina e quimotripsina onde a forma nativa mostrou-se resistente à ação enzimática enquanto o aquecimento (96 e 121°C/ 15min) não foi suficiente para aumentar a susceptibilidade à hidrólise, significativamente. Adição de NaCl 0,3M levou a um aumento da estabilidade estrutural com menor susceptibilidade à digestão proteolítica, fato em parte perdido com o aquecimento. As hidrólises foram acompanhadas por eletroforese em gel de poliacrilamida dodecilsulfato de sódio. Palavras-chave: grão-de-bico; Cicer arietinum L.; globulina majoritária; caracterização; hidrólise in vitro. SUMMARY CHARACTERIZATION AND in vitro TRYPTIC HYDROLYSIS OF THE MAJOR GLOBULIN FROM CHICKPEA (Cicer arietinum L.).The isolation and characterization of the major globulin fraction (11 S) from Chickpea, vc IAC-Marrocos, were evaluated. The major globulin was extracted, isolated by gel filtration and ion-exchange chromatography showing only one protein band on PAGE. The globulin, after Sephadex elution, revealed two protein bands of 55 and 52.5kDa and three minor bands on SDS-PAGE. In the presence of 2-mercaptoethanol six polypeptides were revealed on SDS-PAGE in the range of 18 to 42kDa. The isolated native globulin shown to be resistant to trypsin and chymotrypsin however heating at 96 and 121ºC/15min was not sufficient to increase the hydrolysis significantly. The proteolytic susceptibility of the enzymes was reduced by 0.3M NaCl addition at the assay. The salt concentration was sufficient to stabilize the native protein structure that was lost after heating as demonstrated on SDS-PAGE.

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“…Gel filtration has been used (16) and also repeated isoelectric precipitation (2,16 It has been suggested that legumin and vicilin are closely related, have sequences of amino acids in common (16), and that immunologically they cross react reciprocally (19). There are two possible explanations for this cross-reactivity.…”

Section: Isolation and Characterisation Of Legumin And Vicilinmentioning

confidence: 99%

“…Varner and Schidlovsky (29) showed globulins to be localized in protein bodies within pea cotyledons. Jackson et al (16) analyzed legumin and vicilin from Vicia faba L. by fingerprinting tryptic digests and identifying the N-terminal amino acids. The subunits of legumin have been studied by Bailey and Boulter (2).…”

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confidence: 99%

Legumin Synthesis in Developing Cotyledons of Vicia faba L.

1971

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The synthesis of legumin in developing cotyledons of Vicia faba L. has been examined as a potential system for approaching the problem of differential gene expression. The pattern of legumin synthesis was determined during the growth of the cotyledon by microcomplement fixation which provided a sensitive and specific assay for legumin in the presence of vicilin. Legumin was detected even in young cotyledons. However, when the cotyledons were about 10 millimeters long, and cell division was essentially complete, there was a sharp increase in the rate of legumin accumulation.Developing seeds of Leguminosae offer an attractive system for studying the problem of differential gene expression. These seeds accumulate large amounts of globulins which consist of two high molecular weight proteins, legumin and vicilin, as defined by analytical centrifugation (11,12). Varner and Schidlovsky (29) showed globulins to be localized in protein bodies within pea cotyledons. A major attempt to use developing seeds of Leguminosae for studies of differential gene expression was first made by . They used immature seeds of Pisum sativum for analyzing the regulation of transcription and translation of chromatin preparations from cotyledon cells. More recently, Boulter and associates (2,3,9,10,25,32) have initiated extensive studies of cotyledon development in V.faba. In this paper we wish to report our analyses of legumin synthesis in relation to the growth of the cotyledon of V. faba. MATERIAIS AND METHODS Plant Material. Seeds of Vicia faba L. (cultivar unknown)were grown in soil in the greenhouse or garden. When pods were harvested, any abnormally shaped material was excluded. In a pod there were usually three or four seeds of equal size which were used and one or two smaller seeds which were

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A COMPARISON OF SOME PROPERTIES OF VICILIN AND LEGUMIN ISOLATED FROM SEEDS OF PISUM SATIVUM, VICIA FABA AND CICER ARIETINUM

Cited by 77 publications

References 9 publications

Genetic variability in the structure of the α-subunits of legumin from Pisum—a two-dimensional gel electrophoresis study

Genetic variability in the structure of the α-subunits of legumin from Pisum—a two-dimensional gel electrophoresis study

Caracterização e hidrólise in vitro da globulina principal de grão-de-bico (Cicer arietinum L.), var. IAC-Marrocos

Legumin Synthesis in Developing Cotyledons of Vicia faba L.

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