作者: M.J. Coleman , J. Mainzer , A.G. Dickerson
DOI: 10.1016/0885-5765(92)90015-N
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摘要: Abstract A glycoprotein elicitor of phytoalexin accumulation in leaves Phaseolus vulgaris, produced well before lysis the medium cultures Colletotrichum lindemuthianum race δ, has been purified to apparent homogeneity. The was a monomer molecular weight 28 kDa with pI 4·25. glycosyl side chains which accounted for 43% holoprotein, were composed principally galactose, mannose and rhamnose, exhibited minimum degree polymerization 8 apparently O-linked abundant serine and/or threonine residues peptide backbone. In P. vulgaris leaf injection bioassay had activity easily detectable at nanomolar concentrations induced browning treated tissue both phenylalanine ammonia-lyase isoflavonoid phaseollinisoflavan. For these three linked defence responses, suboptimal respectively 4·2, 7·6 9·7 fold more cultivar resistant δ (ev. Kievit) than susceptible that Pinto). Protein integrity not required side-chains isolated from protein shown be active elicitors. role this plant/pathogen interaction is discussed.