Journal article
Screening the recognition properties of peptide hormone sequence mutants by analytical high performance liquid affinity chromatography on immobilized neurophysin
Collection of Czechoslovak chemical communications, v 53(11), pp 2627-2636
1988
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Analytical high performance liquid affinity chromatography with immobilized neurophysin was used as a molecular screen to evaluate the effects of peptide hormone structure modification on protein recognition. Immobilization of neurophysin on silica and highly cross-linked agarose occurred with retention of oxytocin and vasopressin binding properties. The effects of one-residue-at-a-time mutation, multi-site sequence simplification, and sequence randomization of critical contact residues were evaluated by extent of binding of the peptides on the affinity matrix. The analytical chromatography method also was used as a stereoselective detector to identify racemic contaminants in peptide hormone preparations.
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Details
- Title
- Screening the recognition properties of peptide hormone sequence mutants by analytical high performance liquid affinity chromatography on immobilized neurophysin
- Creators
- Giorgio Fassina - National Institute of Diabetes and Digestive and Kidney DiseasesMichal Lebl - Czechoslovak Academy of SciencesIrwin M. Chaiken - National Institute of Diabetes and Digestive and Kidney Diseases
- Publication Details
- Collection of Czechoslovak chemical communications, v 53(11), pp 2627-2636
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; Drexel University
- Web of Science ID
- WOS:A1988R715900016
- Other Identifier
- 991019520715604721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Chemistry, Multidisciplinary