Literature DB >> 2460101

Characterization of epitopes on the cationic peanut peroxidase by four monoclonal antibodies.

C F Hu1, R B van Huystee.   

Abstract

The epitope sites on the cationic peanut peroxidase were characterized by four monoclonal antibodies raised against this isozyme. Evidence is presented showing that the epitope for monoclonal antibody 1B is located on the polypeptide. Sensitivity of the epitopes recognized by 1M and 2F to 0.1M HCl, boiling, 10 mM periodate and trifluoromethane sulfonic acid treatment indicate that they occur at regions where oligosaccharides are linked to the polypeptide backbone. The antigenic specificity of 2A is, in addition, dependent on the conformation of the epitope site which is destroyed after partial proteolysis of the peroxidase.

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Year:  1988        PMID: 2460101     DOI: 10.1016/s0006-291x(88)80869-6

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

Review 1.  Glycans of higher plant peroxidases: recent observations and future speculations.

Authors:  R B van Huystee; M T McManus
Journal:  Glycoconj J       Date:  1998-02       Impact factor: 2.916

2.  Hormonal regulation and distribution of peroxidase isoenzymes in the Cucurbitaceae.

Authors:  F B Abeles; C L Biles; L J Dunn
Journal:  Plant Physiol       Date:  1989-12       Impact factor: 8.340

3.  Role of carbohydrate moieties in peanut (Arachis hypogaea) peroxidases.

Authors:  C F Hu; R B van Huystee
Journal:  Biochem J       Date:  1989-10-01       Impact factor: 3.857

  3 in total

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