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Purification and Characterization of a Polygalacturonase-Inhibiting Protein from Phaseolus vulgaris L.

Homogeneous endo-polygalacturonase (PG) was covalently bound to cyanogen-bromide-activated Sepharose, and the resulting PG-Sepharose conjugate was utilized to purify, by affinity chromatography, a protein from Phaseolus vulgaris hypocotyls that binds to and inhibits PG. Isoelectric focusing of the p...

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Hlavní autoři: Cervone, Felice, De Lorenzo, Giulia, Degrà, Luisa, Salvi, Giovanni, Bergami, Mario
Médium: Artigo
Jazyk:Inglês
Vydáno: 1987
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1054313/
https://ncbi.nlm.nih.gov/pubmed/16665751
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