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Hankins CN, Herman EM, Kindinger J, et al. The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum. Plant Physiol. 1991;96(1):98-103doi: 10.1104/pp.96.1.98.
Hankins, C. N., Herman, E. M., Kindinger, J., & Shannon, L. M. (1991). The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum. Plant physiology, 96(1), 98-103. https://doi.org/10.1104/pp.96.1.98
Hankins, C N, et al. "The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum." Plant physiology vol. 96,1 (1991): 98-103. doi: https://doi.org/10.1104/pp.96.1.98
Hankins CN, Herman EM, Kindinger J, Shannon LM. The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum. Plant Physiol. 1991 May;96(1):98-103. doi: 10.1104/pp.96.1.98. PMID: 16668191; PMCID: PMC1080718.
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Plant Physiol. 1991 May;96(1):98-103. doi: 10.1104/pp.96.1.98.

The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum.

Plant physiology

C N Hankins, E M Herman, J Kindinger, L M Shannon

Affiliations

  1. Department of Biochemistry, University of California, Riverside, Riverside, California 92521.

PMID: 16668191 PMCID: PMC1080718 DOI: 10.1104/pp.96.1.98

Abstract

The seeds of Spartium junceum contained a large quantity of lectin-like protein that did not appear to be either a hemagglutinin or active lectin. The cross-reactive material (CRM), like most legume seed lectins, was a tetrameric glycoprotein of about 130,000 M(r). The singlesized subunits of about 33,000 M(r) were not covalently associated. The amino acid composition was typical of legume lectins and was rich in hydroxy-amino acids and poor in sulfur-containing amino acids. The Spartium CRM contained about 3.5% covalently associated carbohydrate, most likely of the high-mannose type, since the CRM was precipitated by concanavalin A. The CRM was localized by electron-microscopic immunocytochemistry and found to be exclusively in protein-filled vacuoles (protein bodies). Because this protein was so similar immunologically, structurally, and in its physiology, to classic legume seed lectins, it is most likely a lectin homolog. Similar seed lectin CRMs appear to be both common and widespread in the Leguminosae.

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