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Lectins in castor bean seedlings.

S M Harley1, H Beevers

  • 1Biology Department, University of California, Santa Cruz, California 95064.

Plant Physiology
|January 1, 1986
PubMed
Summary
This summary is machine-generated.

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Castor bean seedlings degrade ricin and Ricinus communis agglutinin lectins during germination. These lectins are not detected in green cotyledons or aerial parts of mature seedlings.

Area of Science:

  • Plant Biochemistry
  • Molecular Biology

Background:

  • Lectins, including ricin and Ricinus communis agglutinin, are storage proteins in castor bean seeds.
  • Their role and degradation during seedling development are not fully understood.

Purpose of the Study:

  • To quantify ricin and Ricinus communis agglutinin lectins in castor bean seedlings during germination and early growth.
  • To investigate the susceptibility of these lectins to hydrolysis by endogenous enzymes.

Main Methods:

  • Lectins were quantified using Sepharose chromatography and immunodiffusion with specific antibodies.
  • Hydrolysis assays were performed using isolated proteinases and glycosidases from seedling endosperm.
  • Subunit separation of ricin was achieved using 2-mercaptoethanol and cysteine.

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Main Results:

  • The endosperm lectin content decreased by 50% within 4 days of germination, with complete consumption coinciding with tissue depletion.
  • Lectins were present in low amounts in dry cotyledons but absent in green cotyledons of 10-day-old seedlings.
  • No lectins were detected in aerial parts of 3-week-old seedlings or in endosperm tissue culture.
  • While intact lectins were resistant to hydrolysis, their separated subunits were slowly degraded by proteinases, and glycosidases released mannose.

Conclusions:

  • Castor bean lectins are actively degraded during seedling development, with their disappearance linked to tissue consumption and seedling maturation.
  • The degradation pathway may involve initial subunit separation followed by proteolysis.
  • Light exposure appears to inhibit lectin accumulation in cotyledons.