Embryonal antigens in maize caryopses: The temporal order of antigen accumulation during embryogenesis

Хавкин, Э. Е.; Misharin, S. I.; Ivanov, Vladimir N.; Danovich, K N

doi:10.1007/bf00384894

Cited by 17 publications

(6 citation statements)

References 9 publications

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“…These glycoproteins are of interest from several points of view: firstly, macromolecules of the pollen wall have been implicated in the recognition of pollen by a compatible stigma (Heslop-Harrison, 1975); the glycoproteins studied are present in the pollen wall (Knox et al, 1980) and may be involved in the pollen-stigma recognition. Secondly, both glycoproteins are effective antigens in rabbits; increasingly, immunological techniques are being used to demonstrate markers of identity in plants (Raff et al, 1980) and to monitor molecular changes associated with differentiation (Khavkin et al, 1977(Khavkin et al, , 1979, although the antigens involved have not been chemically defined. The present study contributes to our understanding of the nature of antigenic plant macromolecules.…”

mentioning

confidence: 99%

Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen

Howlett¹,

Clarke²

1981

Biochemical Journal

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Two glycoproteins have been purified from a buffer extract of rye-grass (Lolium perenne) pollen. Both migrated as single bands on sodium dodecyl sulphate/polyacrylamide gels. Glycoprotein 1 (0.8 mg/g of pollen) had a apparent mol.wt. of 33 000 and contained 95% protein and 5% carbohydrate. The monosaccharides glucose, galactose, mannose, arabinose and N-acetylglucosamine were present in the proportions 3:3:1:2:1. Glycoprotein 2 (0.4 mg/g of pollen) had an apparent mol. wt. of 68000 and contained 88% protein and 12% carbohydrate. The monosaccharides glucose, galactose, mannose, fucose, xylose, arabinose and N-acetylglucosamine were present in the proportions 4:7:13:5:8:6:6. This glycoprotein bound concanavalin A and Lotus tetragonolobus (asparagus pea) lectin. Radioallergosorbent (RAST) inhibition tests showed that Glycoprotein 1 is an effective allergen, whereas Glycoprotein 2 has less allergenic activity. A method for performing both lectin-binding assays and RAST inhibition tests using microtitre trays is described.

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Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen

Howlett¹,

Clarke²

1981

Biochemical Journal

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“…These may involve proteins similar to legumin. Globulins resembling those of legumes have been reported to occur in corn (maize, Zea mays) (Khavkin et al, 1977). In addition, the glutelin fraction of rice was recently shown to possess polypeptides homologous with pea legumin (Zhao et al, 1983).…”

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confidence: 99%

Homology between legumin-like polypeptides from cereals and pea

Robert¹,

Nozzolillo²,

Altosaar³

1985

Biochemical Journal

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The presence of legumin-like constituents within the globulin fractions of wheat (Triticum aestivum), rye (Secale cereale) and corn (maize, Zea mays) was demonstrated. Two-dimensional analysis of wheat globulins in the presence and absence of a reducing agent revealed the existence of reducible approximately 60 kDa polypeptides. Western-blot analysis with 125I-labelled antibodies raised against the oat (Avena sativa) 12S globulin holoprotein or its alpha-subunits demonstrated, firstly, the immunological homology between the alpha- and beta-subunits of pea (Pisum sativum) legumin and oat 12S globulin, and secondly, the similar occurrence in wheat of antigenically homologous approximately 20kDa and approximately 40 kDa polypeptides that associate via disulphide linkage to form approximately 60 kDa dimers. Western blotting also showed the presence of disulphide-linked approximately 20 kDa and approximately 40 kDa legumin-like subunits within the globulin fractions of rye and corn.

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“…Em milho, o mecanismo de embriogênese somática foi comprovado pelos trabalhos de LU et alii (1982; 1983), GREEN (1982). GREEN et alii (1983).…”

Section: Páginaunclassified

“…Genetica Warsaw, 23: 93-101. 1982. Kat-yotype stability of haploid ano diploid maize root tissue cultures.…”

Section: Armstrong CLmentioning

confidence: 99%

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Cultivo in vitro de milho (>i<Zea mays>/i< L.) e análise da sua instabilidade mitótica

Fluminhan¹

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Embryonal antigens in maize caryopses: The temporal order of antigen accumulation during embryogenesis

Cited by 17 publications

References 9 publications

Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen

Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen

Homology between legumin-like polypeptides from cereals and pea

Cultivo in vitro de milho (>i<Zea mays>/i< L.) e análise da sua instabilidade mitótica

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