Affiliation:
1. Department of Biology, Semmelweis University of Medicine, H-1445 Budapest Magyvárad tér 4, POB 370, Hungary
Abstract
Insulin and its A and B chain increased the quantity of intracellular PAS-positive material (glycogen) in tetrahymena, whereas the combined A+B chains decreased it. Imprinting—previous interaction—with insulin, its A and B chains in themselves and with the A+B chain increased the hormone binding capacity of tetrahymena, but the functional effect of imprinting (storage or breakdown of glycogen) showed a different tendency with insulin and A+B chain on the one hand, and A chain and B chain on the other. Since the imprinting potential of a molecule promotes the induction of receptor formation, the fact remains that both component chains of insulin were able to act as potential imprinters, although the A chain was superior to the B chain in this respect throughout, and combined treatment with the A+B chain ultimately induced the formation of a similar binding site as insulin itself.
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference18 articles.
1. Csaba, G. (1985)Int. Rev. Cytol. 95:327?377.
2. Csaba, G. (1986)Experientia 42:715?718.
3. Csaba, G. (1980)Biol. Rev. 55:47?63.
4. Csaba, G. (1981)Ontogeny and phylogeny of hormone receptors. Karger, Basel, New York.
5. Csaba, G. and Nagy, S. U. (1976)Acta biol meg. germ. 35:1399?1401.
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