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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 125 (1998), S. 471-473 
    ISSN: 1573-8221
    Keywords: Progesterone ; progesterone receptor ; progesterone analog ; steroid-receptor interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Binding of3H-16α, 17α-cyclopropanoprogesterone (CPG) and3H-progesterone (PG) to progesterone receptors in soluble fraction of rat uterus is studied. It is shown that CPG and PG specifically bind to the protein with similar affinity and binding capacity. Unlabeled PG competitively inhibits the binding of CPG, and unlabeled CPG competitively inhibits the binding of PF with the same efficiency. Dissociation of CPG- and PG-receptor complexes is characterized by the same dissociation constant.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Fusicoccin (activity, binding) ; Plasmalemma (fusicoccin binding) ; Protoplast (fusicoccin binding) ; Vicia (fusicoccin binding) ; Zea (fusicoccin binding)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The concentration dependences of the binding of fusicoccins (FCs) A, B, C, D, J and H to plasma membranes isolated from maize (Zea mays L.) roots have been studied in parallel with the effects of these compounds on elongation and 86Rb transport in detached maize roots. The dissociation constants obtained showed a good correlation between the affinity of the FCs for the plasmalemma and their biological activity. However, the range of physiologically active FC concentrations proved to be about two orders of magnitude higher than that calculated from the dissociation constants. It was also shown that Vicia faba L. mesophyll protoplasts, unlike isolated plasma membranes, have two FC-binding sites, one with a K D similar to that of the isolated plasmalemma while the other has a substantially higher K D , apparently corresponding to the physiologically active state of the FC-binding proteins.
    Type of Medium: Electronic Resource
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