An N-terminal Peptide Extension Results in Efficient Expression, but not Secretion, of a Synthetic Horseradish Peroxidase Gene in Transgenic Tobacco | Zendy

Mihály Kis | Zendy

Open Access

An N-terminal Peptide Extension Results in Efficient Expression, but not Secretion, of a Synthetic Horseradish Peroxidase Gene in Transgenic Tobacco

Author(s) -

Mihály Kis

Publication year - 2004

Publication title -

annals of botany

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.567

H-Index - 176

eISSN - 1095-8290

pISSN - 0305-7364

DOI - 10.1093/aob/mch045

Subject(s) - biology , horseradish peroxidase , peroxidase , transgene , secretion , peptide , gene , signal peptide , isozyme , biochemistry , terminal (telecommunication) , genetically modified crops , microbiology and biotechnology , enzyme , peptide sequence , telecommunications , computer science

Native horseradish (Armoracia rusticana) peroxidase, HRP (EC 1.11.1.7), isoenzyme C is synthesized with N-terminal and C-terminal peptide extensions, believed to be associated with protein targeting. This study aimed to explore the specific functions of these extensions, and to generate transgenic plants with expression patterns suitable for exploring the role of peroxidase in plant development and defence.

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