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Hormonotoxins I. Strategy for synthesis of ovine luteinizing hormone - gelonin conjugate bearing the toxin in the β-subunit
- Source :
- International Journal of Peptide and Protein Research. 33:22-28
- Publication Year :
- 2009
- Publisher :
- Wiley, 2009.
-
Abstract
- The amino groups in the beta-subunit of ovine luteinizing hormone (oLH) were modified by thiolation using N-succinimidyl-3-(2-pyridyldithio) propionate so that it may be coupled in a disulfide linkage to similarly modified ribosome inactivating protein, gelonin. The modified beta-subunit was able to hybridize with free LH alpha-subunit and the complex retained full biological activity. However, when gelonin was coupled to the beta-subunit, the resulting conformational changes masked or eliminated the sites necessary for intersubunit recognition of the free alpha-subunit. This has important implications for the design in the synthesis of gonadotropin-toxin/drug conjugates.
- Subjects :
- chemistry.chemical_classification
Binding Sites
Sheep
Protein Conformation
Disulfide Linkage
medicine.drug_class
Ribosome-inactivating protein
Succinimides
Biological activity
Luteinizing Hormone
Biochemistry
chemistry
Drug Design
Ribosome Inactivating Proteins, Type 1
Propionate
medicine
Animals
Gelonin
Gonadotropin
Luteinizing hormone
Plant Proteins
Conjugate
Subjects
Details
- ISSN :
- 03678377
- Volume :
- 33
- Database :
- OpenAIRE
- Journal :
- International Journal of Peptide and Protein Research
- Accession number :
- edsair.doi.dedup.....20ac89231caf3ef58a00f2f244d19916