| pubmed-article:16665750 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16665750 | lifeskim:mentions | umls-concept:C0004039 | lld:lifeskim |
| pubmed-article:16665750 | lifeskim:mentions | umls-concept:C0996865 | lld:lifeskim |
| pubmed-article:16665750 | lifeskim:mentions | umls-concept:C0027540 | lld:lifeskim |
| pubmed-article:16665750 | lifeskim:mentions | umls-concept:C1881065 | lld:lifeskim |
| pubmed-article:16665750 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
| pubmed-article:16665750 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16665750 | pubmed:dateCreated | 2010-6-29 | lld:pubmed |
| pubmed-article:16665750 | pubmed:abstractText | Endo-polygalacturonase (PG) was purified from a commercial preparation of Aspergillus niger pectinase by means of carboxymethylcellulose chromatography, preparative isoelectric focusing, and gel permeation through Sephadex G-50. The enzyme was electrophoretically homogeneous and consisted of a single polypeptide chain with a molecular weight of 33,500. The enzyme exhibited a specific activity significantly higher than those of purified polygalacturonases from phytopathogenic fungi. Galacturonate oligomers with a degree of polymerization higher than four appeared quickly as products of the enzymic hydrolysis of Napolygalacturonate. The oligomers were later degraded to di- and monogalacturonate. The homogeneous enzyme and growing mycelium of Aspergillus niger separately elicited a necrotic response in cowpea (Vigna unguiculata Walp.) pods. Heat-inactivated PG and PG inactivated with specific antibodies did not elicit necrosis, suggesting that the catalytic activity of the enzyme is necessary for its function as an elicitor. The PG-released oligosaccharides from Vigna cell wall and the galacturonides with a degree of polymerization greater than four separately elicited necrosis, whereas di- and monogalacturonate did not. | lld:pubmed |
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| pubmed-article:16665750 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16665750 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16665750 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:16665750 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16665750 | pubmed:issn | 0032-0889 | lld:pubmed |
| pubmed-article:16665750 | pubmed:author | pubmed-author:CervoneFF | lld:pubmed |
| pubmed-article:16665750 | pubmed:author | pubmed-author:SalviGG | lld:pubmed |
| pubmed-article:16665750 | pubmed:author | pubmed-author:De LorenziAA | lld:pubmed |
| pubmed-article:16665750 | pubmed:author | pubmed-author:DegràLL | lld:pubmed |
| pubmed-article:16665750 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16665750 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:16665750 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16665750 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16665750 | pubmed:pagination | 626-30 | lld:pubmed |
| pubmed-article:16665750 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
| pubmed-article:16665750 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:16665750 | pubmed:articleTitle | Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by alpha-d-Galacturonate Oligomers. | lld:pubmed |
| pubmed-article:16665750 | pubmed:affiliation | Dipartimento di Biologia vegetale, Università di Roma "La Sapienza," Piazzale A. Moro 00100, Rome, Italy. | lld:pubmed |
| pubmed-article:16665750 | pubmed:publicationType | Journal Article | lld:pubmed |
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