α-l-arabinofuranosidases and β-d-galactosidases in germinating-lupin cotyledons

Matheson, Norman K.; Saini, H.S.

doi:10.1016/s0008-6215(00)81924-2

Cited by 24 publications

(14 citation statements)

References 30 publications

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“…In the pH range 2.5-6.5 the maximum enzyme activity varied among the three β-galactosidase rich fractions: 3.5-4.5 for β-gal I, 3.0-3.5 for β-gal II, and 3.0-4.0 for β-gal III (figure 2). These results are similar to those found for cotyledonary β-galactosidases from Vigna sinensis (Biswas 1987) and Vigna radiata (Kundu et al 1990), as well as for seeds (Agrawal & Bahl 1968, Li et al 1975, Matheson & Saini 1977 al. 1988, Sekimata et al 1989, Giannakouros et al 1991, Buckeridge & Reid 1994, shoots (Konno & Tsumuki 1993), leaves (Sawicka & Kacperska 1995) and fruits (Pressey 1983, Ogawa et al 1990, Ranwala et al 1992) of different species.…”

Section: Resultssupporting

confidence: 86%

“…enzymes acting at β-galactosydic bonds of both oligo-and polysaccharides. Although they are widely distributed in plants (Wallenfels & Malhotra 1961) their physiological role is still not well understood (Li et al 1975, Matheson & Saini 1977, Revta brasil. Bot., São Paulo, V.23, n.1, p.69-76, mar.…”

Section: Resumo -(Múltiplas Formas De β-Galactosidases Cotiledonares mentioning

confidence: 99%

“…2000Sekimata et al 1989, Simos et al 1989, Kundu et al 1990, Giannakouros et al 1991, Enéas-Filho et al 1995. It has been suggested that these enzymes are associated to the depletion of oligo-and polysaccharides during the initial phases of seed germination (Matheson & Saini 1977, Corchete & Guerra 1986, Biswas 1987, Enéas-Filho et al 1995, involved in the metabolism of cell wall constituints (Corchete & Guerra 1987a, Edwards et al 1988, Dopico et al 1989, Konno & Katoh 1992, Konno & Tsumuki 1993, Gómez et al 1995, Kitagawa et al 1995, and in the process of fruit ripening (Pressey 1983, Ogawa et al 1990, Veau et al 1993, Ali et al 1995. β-galactosidase activity has been detected in quiescent seeds (Dey 1984) as well as during germination and seedling establishment (Agrawal & Bahl 1968, Corchete & Guerra 1987b, Kundu et al 1990, Buckeridge & Reid 1994, Enéas-Filho et al 1995.…”

Section: Resumo -(Múltiplas Formas De β-Galactosidases Cotiledonares mentioning

confidence: 99%

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Multiple forms of cotyledonary b-galactosidases from Vigna unguiculata quiescent seeds

Enéas-Filho¹,

Sudério²,

Gomes-Filho³

et al. 2000

Rev. bras. Bot.

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-(Multiple forms of cotyledonary β-galactosidases from Vigna unguiculata quiescent seeds). Cotyledonary β-galactosidases were isolated and partially purified from Pitiúba cowpea (Vigna unguiculata (L.) Walp.) quiescent seeds. The purification steps consisted of precipitation of the crude extract with ammonium sulphate in the range of 20-60% saturation, acid precipitation, DEAE-Sephadex ion-exchange chromatography and Lactosyl-Sepharose affinity chromatography. This purification process gave rise to three β-galactosidases-rich fractions: β-gal I, β-gal II and β-gal III, which were purified about 5, 509, and 62 fold, respectively. They reached maximal enzyme activity at different pH ranges: 3.5-4.5 for β-gal I, 3.0-3.5 for β-gal II, and 3.0-4.0 for β-gal III. Their maximal activities were reached when the temperature of the assay medium was 60°C, and preincubation of the enzymes at different temperatures has shown that they were heat-stable up to 50°C. There were no significant differences among the partially purified enzymes as to their response to the different effectors tested, except for Mn 2+ and EDTA, which affected β-gal I, β-gal II, and β-gal III differ- other plant β-galactosidases. Although three isoforms of this enzyme were obtained through this purification process, isoelectric focusing in polyacrylamide slab gel of these enzyme-proteins suggests that cotyledons of Pitiúba cowpea quiescent seeds possess four isoforms of β-galactosidases. RESUMO -(Múltiplas formas de β-galactosidases cotiledonares de sementes quiescentes de Vigna unguiculata).β-galactosidases cotiledonárias foram isoladas e purificadas, parcialmente, de sementes quiescentes de feijão-de-corda (Vigna unguiculata (L.) Walp.) Pitiúba. As etapas de purificação consistiram de precipitação do extrato bruto com sulfato de amônio na faixa de 20-60% de saturação, precipitação ácida, cromatografia de troca-iônica em DEAE-Sephadex e cromatografia de afinidade em Lactosil-Sepharose. Esse processo de purificação deu origem a três frações ricas em β-galactosidases: β-gal I, β-gal II e β-gal III, as quais foram purificadas cerca de 5, 509 e 62 vezes, respectivamente. Elas atingiram máxima atividade enzimática em diferentes faixas de pH: 3,5-4,5 para β-gal I, 3,0-3,5 para β-gal II e 3,0-4,0 para β-gal III. Suas atividades máximas foram alcançadas quando a temperatura do meio de ensaio era 60°C, e a preincubação das enzimas em diferentes temperaturas mostrou que elas eram termoestáveis até 50°C. Não houve diferenças significativas entre as enzimas parcialmente purificadas no que respeita à resposta dos diferentes efetores testados, exceto para Mn 2+ e EDTA, que afetaram, diferentemente, β-gal I, β-gal II e β-gal III. . Essas propriedades químicas e físicas são semelhantes às encontradas para outras β-galactosidases de plantas. Embora três isoformas dessa enzima tenham sido obtidas através desse processo de purificação, a focalização isoelétrica em placa de gel de poliacrilamida dessas proteinas enzimáticas sugere que cotilédones de sementes qu...

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Section: Resultssupporting

confidence: 86%

Section: Resumo -(Múltiplas Formas De β-Galactosidases Cotiledonares mentioning

confidence: 99%

Section: Resumo -(Múltiplas Formas De β-Galactosidases Cotiledonares mentioning

confidence: 99%

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Multiple forms of cotyledonary b-galactosidases from Vigna unguiculata quiescent seeds

Enéas-Filho¹,

Sudério²,

Gomes-Filho³

et al. 2000

Rev. bras. Bot.

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“…These values are comparable with those of (3-Galases from such plant tissues as jack bean (75 kD) (19), nasturtium seeds (97 kD) (9), Vigna sinensis seeds (43.6, 66.8, 54.3, 79.4 kD) (5), and lupin cotyledons (74, 65, 54 kD) (20).…”

Section: Discussionsupporting

confidence: 71%

“…A higher ratio of fi-(80) to a-anomer (20) was obtained in rapidly frozen sample of the hydrolyzate than that (65:35) of the mutarotated sample, providing evidence for the retention of fl-anomeric configuration of the released D-Gal.…”

Section: Mode Of Actionmentioning

confidence: 84%

A β-Galactosidase from Radish (Raphanus sativus L.) Seeds

Sekimata¹,

Ogura²,

Tsumuraya³

et al. 1989

Plant Physiol.

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A basic,8-galactosidase (,8-Galase) has been purified 281-fold from imbibed radish (Raphanus sativus L.) seeds by conventional purification procedures. The purified enzyme is an electrophoretically homogeneous protein consisting of a single polypeptide with an apparent molecular mass of 45 kilodaltons and pi values of 8.6 to 8.8. The enzyme was maximally active at pH 4.0 on pnitrophenyl 8-D-galactoside and 8l-1,3-linked galactobiose. The enzyme activity was inhibited strongly by Hg2 and 4-chloromercuribenzoate. D-Galactono-(1_-4)-lactone and D-galactal acted as potent competitive inhibitors. Using galactooligosacchandes differing in the types of linkage as the substrates, it was demonstrated that radish seed ,B-Galase specifically split off j0-1,3-and ,8-1,6-linked D-galactosyl residues from the nonreducing ends, and their rates of hydrolysis increased with increasing chain lengths. Radish seed and leaf arabino-3,6-galactan-proteins were resistant to the 0-galase alone but could be partially degraded by the enzyme after the treatment with a fungal a-L-arabinofuranosidase leaving some oligosaccharides consisting of D-galactose, uronic acid, L-arabinose, and other minor sugar components besides D-galactose as the main product.,3-Galactosidases (EC 3.2.1.23) are widely distributed in various plant tissues (8). The enzymic properties, multiple forms, and specificities relevant to structural studies on glycoproteins have been investigated (2,8,19). Recently, interest in this enzyme has been focused on its in vivo functions concerning the degradation of such galactose-containing cell wall polysaccharides as galactan-pectin polymers and xyloglucan in relation to cell growth (16), fruit ripening (25), and seed germination (9). Further, characterization of a thylakoid bound f,-Galase' in wheat leaf chloroplasts implicated the role for the intermediary degradation of mono-and digalactosylglycerol abundant in thylakoid membranes during senescence of chloroplasts (4).Working with organs that develop after germination of radish seeds, we have recently reported the formation of organ-specific AGPs in primary and mature roots and leaves, which were clearly distinguishable from the seed proteogly-' Abbreviations: ,8-Galase, ,B-galactosidase; PNP-P-DGal, p-nitrophenyl l-D-galactoside; ONP-,#--Gal, o-nitrophenyl ,-D-galactoside; 4-MU-fl-n-Gal, 4-methylumbelliferyl fl-Dgalactoside; X-Gal, 5-bromo4-chloro-3-indolyl t-n-galactoside; AG, arabinogalactan; AGP, arabinogalactan-protein; a-L-Arafase, a-L-arabinofuranosidase; 2-ME, 2-mercaptoethanol. 567 cans in chemical composition, structure, and serological properties (21,30,31).In the present paper, we report the purification and characterization of a radish seed ,B-Galase whose specificity is highly restricted to f3-1,3-and :3-1,6-linked D-galactosyl residues, thereby participating in the degradation ofthe backbone structure of radish AGPs. MATERIALS AND METHODS Plant MaterialSeeds of the radish (Raphanus sativus L. var hortensis cv Aokubi) were purchased from Tokita Seed ...

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Biochemistry of the Multiple Forms of Glycosidases in Plants

1984

Advances in Enzymology - And Related Areas of Molecular Biology

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α-l-arabinofuranosidases and β-d-galactosidases in germinating-lupin cotyledons

Cited by 24 publications

References 30 publications

Multiple forms of cotyledonary b-galactosidases from Vigna unguiculata quiescent seeds

Multiple forms of cotyledonary b-galactosidases from Vigna unguiculata quiescent seeds

A β-Galactosidase from Radish (Raphanus sativus L.) Seeds

Biochemistry of the Multiple Forms of Glycosidases in Plants

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