ISOLATION, PURIFICATION AND CRYSTALLIZATION OF AVIAN AND FISH INSULINS

Autor: D. I. Ostrovskii, O. A. Yunev, L. V. Dmitrenko
Rok vydání: 1976
Předmět:
DOI: 10.1016/b978-0-08-021257-9.50031-0
Popis: Insulin has been obtained from the pancreases of chicken and Scorpaena (scorpionfish). Chemical purity of the preparations has been confirmed by the disk-electrophoresis in polyacryl amide gel and N-terminal amino acids determination. The purity of hormones is also confirmed by the coincidence of UV spectra of the porcine (control), avian, and fish insulins and their absorption maximum at 278 nm. N-terminal amino acids both of chicken and Scorpaena insulins are glycine (A-chain) and alanine (B-chain). Chicken insulin biological activity, evaluated by the convulsive reaction of mice in vivo , is equal to 22.8 ± 3.2 µU/mg; scorpaena insulin activity is somewhat lower in this test (18.6 ± 2.2 µU/mg). “Dose-response” curves for porcine and chicken insulins, when comparing their biological acitvity in vitro (by the rat diaphragm and epididymal fat methods) coincide. The fish insulin is less potent in low doses with respect to its effect on muscular and adipose tissues of rat than the porcine hormone. The maximum effect on muscular and adipose tissues is, however, reached with the same doses of the porcine and fish hormones.
Databáze: OpenAIRE