Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1983 Mar;71(3):460–465. doi: 10.1104/pp.71.3.460

β-1,3-Endoglucanase from Soybean Releases Elicitor-Active Carbohydrates from Fungus Cell Walls

N T Keen 1, M Yoshikawa 1
PMCID: PMC1066060  PMID: 16662849

Abstract

Two enzymes from soybean (Glycine max L. Merr. cv Harosoy 63) cotyledons released elicitor-active carbohydrates from cell walls of the phytopathogenic fungus Phytophthora megasperma f.sp. glycinea. They were identified as isoenzymes of β-1,3-endoglucanase (EC 3.2.1.39) with isoelectric points of pH 8.7 and 10.5. The pI 10.5 enzyme was extracted in the greatest amount and was isolated as a homogeneous protein of about 33,000 daltons as determined by gel filtration and sodium dodecyl sulfategel electrophoresis. The purified enzymes hydrolyzed several β-1,3-glucans in a strictly random manner, but degraded neither β-1,6- nor β-1,4-glucans.

Full text

PDF
460

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abeles F. B., Bosshart R. P., Forrence L. E., Habig W. H. Preparation and purification of glucanase and chitinase from bean leaves. Plant Physiol. 1971 Jan;47(1):129–134. doi: 10.1104/pp.47.1.129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bartnicki-Garcia S. Chemistry of hyphal walls of Phytophthora. J Gen Microbiol. 1966 Jan;42(1):57–69. doi: 10.1099/00221287-42-1-57. [DOI] [PubMed] [Google Scholar]
  3. Cline K., Albersheim P. Host-Pathogen Interactions : XVII. HYDROLYSIS OF BIOLOGICALLY ACTIVE FUNGAL GLUCANS BY ENZYMES ISOLATED FROM SOYBEAN CELLS. Plant Physiol. 1981 Jul;68(1):221–228. doi: 10.1104/pp.68.1.221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cline K., Albersheim P. Host-Pathogen Interactions: XVI. PURIFICATION AND CHARACTERIZATION OF A beta-GLUCOSYL HYDROLASE/TRANSFERASE PRESENT IN THE WALLS OF SOYBEAN CELLS. Plant Physiol. 1981 Jul;68(1):207–220. doi: 10.1104/pp.68.1.207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Keen N. T., Yoshikawa M., Wang M. C. Phytoalexin Elicitor Activity of Carbohydrates from Phytophthora megasperma f.sp. glycinea and Other Sources. Plant Physiol. 1983 Mar;71(3):466–471. doi: 10.1104/pp.71.3.466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  7. Nichols E. J., Beckman J. M., Hadwiger L. A. Glycosidic Enzyme Activity in Pea Tissue and Pea-Fusarium solani Interactions. Plant Physiol. 1980 Aug;66(2):199–204. doi: 10.1104/pp.66.2.199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Tepfer M., Taylor I. E. The permeability of plant cell walls as measured by gel filtration chromatography. Science. 1981 Aug 14;213(4509):761–763. doi: 10.1126/science.213.4509.761. [DOI] [PubMed] [Google Scholar]
  9. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  10. Yoshikawa M., Matama M., Masago H. Release of a Soluble Phytoalexin Elicitor from Mycelial Walls of Phytophthora megasperma var. sojae by Soybean Tissues. Plant Physiol. 1981 May;67(5):1032–1035. doi: 10.1104/pp.67.5.1032. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES