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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Biochimica et Biophy...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Biochimica et Biophysica Acta (BBA) - Protein Structure
Article . 1978 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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Isolectins of Phaseolus vulgaris. Physicochemical studies

Authors: Arpad Pusztai; James C. Stewart;

Isolectins of Phaseolus vulgaris. Physicochemical studies

Abstract

By a combination of solubility fractionation, continuous free-flow high voltage electrophoresis, molecular sieve and affinity chromatography on fetuin-Sepharose 4B, several lectin fractions of different isoelectric point were obtained from the seeds of Phaseolus vulgaris cv. "Processor". The albumin isolectin range comprised of five major lectin components with isoelectric points between pH 4.6 and 5.2, while the partly overlapping globulin isolectins contained several more lectin components with higher isoelectric points. The two groups had similar amino acid and sugar composition but were only partially identical by immunochemical criteria. The isolectins were also shown to be similar by physicochemical measurements with a common protomer weight value of about 119000. Values of so20,w, 6.84 and 6.76 S, and of V av, 0.712 and 715 ml/g, for the albumin and the globulin lectins, respectively, also indicated a close similarity. Both groups contained, in a slow equilibrium with the protomer, just over 10% of dimer and oligomers. In addition, the albumin lectins also contained a small, 2 S, dissociation product in a slow equilibrium with the protomer. The hydrodynamic data obtained for the albumin isolectins: [eta] = 0.063 dl/g; beta = 2.42 . 10(6) and f/fo = 1.56 indicated a highly voluminous particle with an effective volume of 8.6 . 10(-18) ml. This type of molecular arrangement was general for the major P. vulgaris seed glycoproteins and was, thus, suggested to be of potential importance for their physiological functioning during seed maturation and germination.

Related Organizations
Keywords

Molecular Weight, Protein Conformation, Viscosity, Lectins, Seeds, Hemagglutination Tests, Amino Acids, Isoelectric Focusing, Plant Lectins, Immunoelectrophoresis, Two-Dimensional

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
57
Average
Top 10%
Top 10%
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