The effect of modifications of the A5 and A19 amino acid residues on the biological activity of insulin. [Leu5-A] and [Phe19-A] sheep insulins
- 1 April 1983
- journal article
- research article
- Published by Springer Nature in Protein Journal
- Vol. 2 (2) , 147-170
- https://doi.org/10.1007/bf01025378
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- The importance of the B10 amino acid residue to the biological activity of insulin. [Lys10-B] human insulinProtein Journal, 1982
- Divergence of the in vitro biological activity and receptor binding affinity of a synthetic insulin analog. [21-Asparaginamide-A]insulinBiochemistry, 1980
- [A14-Phenylalanine]Insulin: A New Synthetic AnalogueHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- [A19-Phenylalanine] Insulin: A New Synthetic AnalogueHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- Receptor-binding region of insulinNature, 1976
- Insulin Peptides. XV. The Synthesis of the A Chain of Sheep Insulin and Its Combination with Synthetic or Natural B Chain to Produce Insulin1,2Journal of the American Chemical Society, 1966
- Insulin Peptides. XIV. Synthetic Peptide Derivatives Related to the N-Terminus of the A Chain of Sheep Insulin (Positions 1-9)1,2Journal of the American Chemical Society, 1966
- Insulin Peptides. XIII. The Synthesis of a Dodecapeptide Derivative Containing the C-Terminal Sequence of the A Chain of Sheep Insulin1,2Journal of the American Chemical Society, 1966
- Synthesen in der Polymyxin‐Reihe 9. Mitteilung. Synthese von Polymyxin B1Helvetica Chimica Acta, 1965
- Synthesis of a Biologically Active Analog of Oxytocin, with Phenylalanine Replacing Tyrosine1,2Journal of the American Chemical Society, 1959