Literature DB >> 16661439

Legume: alpha-GALACTOSIDASE FORMS DEVOID OF HEMAGGLUTININ ACTIVITY.

C N Hankins1, J I Kindinger, L M Shannon.   

Abstract

Twenty different legume species (20 genera) were examined for alpha-galactosidase and hemagglutinin activities. Although all of the species contained enzyme activity, only 13 of 20 contained hemagglutinin activities and none displayed a hemagglutinin activity comparable to the previously described alpha-galactosidase-hemagglutinins.The alpha-galactosidase activities in the 20 species possessed remarkably similar kinetic behavior and carbohydrate specificities. All were inhibited by galactose, xylose, and inositol (very similar K(i) values from plant to plant) and had very similar K(m) values for the substrate, p-nitrophenyl alpha-galactoside.Gel filtration analysis of extracts from nine species suggests that legume alpha-galactosidase activities may frequently reside in two molecular weight forms. However, all these species contained a large molecular weight enzyme activity with a size comparable to the alpha-galactosidase-hemagglutinins.Immunochemical studies reveal that the alpha-galactosidases in these plants are immunologically related to an alpha-galactosidase-hemagglutinin and, therefore, are related to one another.These studies suggest that each of the legume species studied (and perhaps all members of this plant family) contain a homologue from a specific class of alpha-galactosidase. Although the previously described alpha-galactosidase-hemagglutinins appear to be members from this enzyme class, these proteins most frequently occur as forms devoid of hemagglutinin activity.

Entities:  

Year:  1980        PMID: 16661439      PMCID: PMC440637          DOI: 10.1104/pp.66.3.375

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  5 in total

1.  The physical and enzymatic properties of a phytohemagglutinin from mung beans.

Authors:  C N Hankins; L M Shannon
Journal:  J Biol Chem       Date:  1978-11-10       Impact factor: 5.157

2.  Legume Lectins: I. Immunological Cross-Reactions between the Enzymic Lectin from Mung Beans and other Well Characterized Legume Lectins.

Authors:  C N Hankins; J I Kindinger; L M Shannon
Journal:  Plant Physiol       Date:  1979-07       Impact factor: 8.340

Review 3.  The lectins: carbohydrate-binding proteins of plants and animals.

Authors:  I J Goldstein; C E Hayes
Journal:  Adv Carbohydr Chem Biochem       Date:  1978       Impact factor: 12.200

4.  Purification and properties of alpha-galactosidases from Vicia faba seeds.

Authors:  P M Dey; J B Pridham
Journal:  Biochem J       Date:  1969-06       Impact factor: 3.857

5.  alpha-D-galactosidase from soybeans destroying blood-group B antigens. Purification by affinity chromatography and properties.

Authors:  N Harpaz; H M Flowers; N Sharon
Journal:  Eur J Biochem       Date:  1977-07-15
  5 in total
  3 in total

1.  Partial purification of a hemagglutinin associated with cell walls from hypocotyls of Vigna radiata.

Authors:  D Haaß; R Frey; M Thiesen; H Kauss
Journal:  Planta       Date:  1981-05       Impact factor: 4.116

2.  Accumulation and Subcellular Localization of alpha-Galactosidase-Hemagglutinin in Developing Soybean Cotyledons.

Authors:  E M Herman; L M Shannon
Journal:  Plant Physiol       Date:  1985-04       Impact factor: 8.340

3.  Identification and immunocytochemical localization of α-galactosidase in resting and germinated date palm (Phoenix dactylifera L.) seeds.

Authors:  K N Sekhar; D A Demason
Journal:  Planta       Date:  1990-04       Impact factor: 4.116

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.