Purification of an Infection-Related, Extracellular Peroxidase from Barley | Zendy

K. Kerby | Zendy; Shauna Somerville | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Purification of an Infection-Related, Extracellular Peroxidase from Barley

Author(s) -

K. Kerby,

Shauna Somerville

Publication year - 1992

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.100.1.397

Subject(s) - hordeum vulgare , peroxidase , extracellular , isoelectric point , isoelectric focusing , biochemistry , antiserum , ion chromatography , powdery mildew , heme , biology , acetone , isozyme , glycoprotein , hemeprotein , chromatography , chemistry , enzyme , botany , poaceae , antibody , immunology

Increases in two extracellular peroxidases were observed following inoculation of barley (Hordeum vulgare L.) with the powdery mildew pathogen (Erysiphe graminis DC.: Fr. f. sp. hordei Em. Marchal). The more prominent isozyme, P8.5, was purified from intercellular wash fluids by acetone precipitation, ion-exchange chromatography, isoelectric focusing, and gel filtration. Purified P8.5 is a heme-containing, glycoprotein with a M(r) of 35,000. It has eight cysteine residues. A highly specific, high-titer antiserum to deglycosylated P8.5 was produced.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research