The structure and physiological activity of a glycoprotein secreted from conidia of Mycosphaerella pinodes. II.
- 1 January 1987
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 35 (1) , 249-255
- https://doi.org/10.1248/cpb.35.249
Abstract
The chemical structure of a glycoprotein secreted from conidia of Mycosphaerella pinodes into the medium during germination was investigated, and its elicitor activity to induce pisatin synthesis in peas was examined. The glycoprotein showed a higher elicitor activity than the intra-conidial polysaccharide. The glycoprotein, whose molecular weight is about 130 .times. 104, has a partial structure in which a reducing terminal mannosyl residue of a trisaccharide .**GRAPHIC**. Glu is O-glycosidically attached to serine in the protein portion.This publication has 3 references indexed in Scilit:
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- Purification and partial characterization of a beta-glucan fragment that elicits phytoalexin accumulation in soybean.Journal of Biological Chemistry, 1984
- The primary structures of one elicitor-active and seven elicitor-inactive hexa(beta-D-glucopyranosyl)-D-glucitols isolated from the mycelial walls of Phytophthora megasperma f. sp. glycinea.Journal of Biological Chemistry, 1984