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Rational Design of Recombinant Papain-Like Cysteine Protease: Optimal Domain Structure and Expressio...

Rational Design of Recombinant Papain-Like Cysteine Protease: Optimal Domain Structure and Expressio...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5535888

Rational Design of Recombinant Papain-Like Cysteine Protease: Optimal Domain Structure and Expression Conditions for Wheat-Derived Enzyme Triticain-α

About this item

Full title

Rational Design of Recombinant Papain-Like Cysteine Protease: Optimal Domain Structure and Expression Conditions for Wheat-Derived Enzyme Triticain-α

Publisher

Switzerland: MDPI

Journal title

International journal of molecular sciences, 2017-06, Vol.18 (7), p.1395

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI

More information

Scope and Contents

Contents

Triticain-α is a papain-like cysteine protease from wheat (
L.) that possesses activity towards toxic gluten-derived peptides, and was thus proposed as a novel therapeutic tool for celiac disease. We report an original approach employing rational design of domain architecture of Triticain-α and selection of the appropriate expression system for...

Alternative Titles

Full title

Rational Design of Recombinant Papain-Like Cysteine Protease: Optimal Domain Structure and Expression Conditions for Wheat-Derived Enzyme Triticain-α

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5535888

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5535888

Other Identifiers

ISSN

1422-0067

E-ISSN

1422-0067

DOI

10.3390/ijms18071395

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