Literature DB >> 7316977

Isolation and properties of a lectin from the seeds of hairy vetch (Vicia villosa Roth).

L Grubhoffer, M Tichá, J Kocourek.   

Abstract

The lectin of the seeds of hairy vetch (Vicia villosa Roth), which selectively binds murine cytotoxic T-lymphocytes, was purified by simple affinity-chromatographic procedures on two different N-acetyl-alpha-D-galactosaminyl-carriers. The lectin thus obtained is homogeneous on polyacrylamide-gel electrophoresis both in acid and alkaline media and has a mol. wt. of approx. 120000. The lectin molecule appears to comprise four subunits of equal electrophoretic mobility, contains 4.3% of covalently bound neutral sugar and 0.72 Mn and 0.94 Zn atoms respectively. The anti-(blood-group A1) specific erythroagglutinating activity of the lectin can be detected at a limit concentration of 15 microgram/ml and is inhibitable most effectively by N-acetyl-D-galactosamine.

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Year:  1981        PMID: 7316977      PMCID: PMC1162933          DOI: 10.1042/bj1950623

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  21 in total

1.  Characterization studies on a new lectin found in seeds of Vicia ervilia.

Authors:  N Fornstedt; J Porath
Journal:  FEBS Lett       Date:  1975-09-15       Impact factor: 4.124

2.  A simple method for the preparation of an affinity absorbent for soybean agglutinin using galactosamine and CH-Sepharose.

Authors:  A K Allen; A Neuberger
Journal:  FEBS Lett       Date:  1975-02-15       Impact factor: 4.124

3.  ACRYLAMIDE GEL ELECTROPHORESIS OF SOLUBLE PLANT PROTEINS: A STUDY ON PEA SEEDLINGS IN RELATION TO DEVELOPMENT.

Authors:  F C STEWARD; R F LYNDON; J T BARBER
Journal:  Am J Bot       Date:  1965-02       Impact factor: 3.844

4.  Purification and characterization of a lectin (plant hemagglutinin) with N blood group specificity from Vicia graminea seeds.

Authors:  M J Prigent; R Bourrillon
Journal:  Biochim Biophys Acta       Date:  1976-01-20

5.  Studies on lectins. XXXII. Application of affinity electrophoresis to the study of the interaction of lectins and their derivatives with sugars.

Authors:  V Horejsí; M Tichá; J Kocourek
Journal:  Biochim Biophys Acta       Date:  1977-09-29

6.  A non-specific phytohemagglutinin found in Vicia cracca.

Authors:  K Aspberg; H Holmén; J Porath
Journal:  Biochim Biophys Acta       Date:  1968-05-06

7.  Purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity.

Authors:  A K Allen; N N Desai; A Neuberger
Journal:  Biochem J       Date:  1976-04-01       Impact factor: 3.857

8.  Purification and properties of blood-group-specific lectins from Vicia cracca.

Authors:  H Rüdiger
Journal:  Eur J Biochem       Date:  1977-01

9.  Studies on lectins. XXXV. Water-soluble O-glycosyl polyacrylamide derivatives for specific precipitation of lectins.

Authors:  V Horejsí; P Smolek; J Kocourek
Journal:  Biochim Biophys Acta       Date:  1978-01-18

10.  Polymerization of proteins with glutaraldehyde. Soluble molecular-weight markers.

Authors:  J W Payne
Journal:  Biochem J       Date:  1973-12       Impact factor: 3.857

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  2 in total

1.  Temporal changes in the carbohydrates expressed on BG01 human embryonic stem cells during differentiation as embryoid bodies.

Authors:  Kimberly A Wearne; Harry C Winter; Irwin J Goldstein
Journal:  Glycoconj J       Date:  2007-08-03       Impact factor: 2.916

2.  The unique enzymatic function of field bean (Dolichos lablab) D-galactose specific lectin: a polyphenol oxidase.

Authors:  Santosh R Kanade; Devavratha H Rao; Ramanath N Hegde; Lalitha R Gowda
Journal:  Glycoconj J       Date:  2008-10-31       Impact factor: 2.916

  2 in total

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