Purification of PRL receptors from toad kidney: Comparisons with rabbit mammary PRL receptors
- Univ. of Geneva School of Medicine (Switzerland) Univ. of Lausanne School of Medicine (Switzerland)
The binding characteristics of the prolactin (PRL) receptors present in toad (Bufo marinus) kidneys were investigated and compared to those of PRL receptors present in rabbit mammary glands. The molecular characteristics of the Triton X-100 solubilized renal and mammary PRL receptors were assessed by gel filtration and by migration analysis on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) after affinity labeling of the binding sites with {sup 125}I-human growth hormone. Similar results were obtained for both receptors. Partial purification of the toad PRL receptor could be achieved by affinity chromatography. The molecular weight of this purified receptor could be determined by analysis of SDS-PAGE. With the use of a polyclonal antiserum raised against a purified preparation of rabbit mammary PRL receptor, one or several antigenic epitope(s) could be identified on the core of the toad renal PRL receptor. In conclusion, although the structure and the biological role(s) of PRL have substantially changed during evolution, the receptor for this hormone has retained many of its structural features as could be assessed between an amphibian and a mammalian species on functionally different target tissues.
- OSTI ID:
- 7101061
- Journal Information:
- American Journal of Physiology; (USA), Vol. 254:3; ISSN 0002-9513
- Country of Publication:
- United States
- Language:
- English
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KIDNEYS
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INTERMEDIATE MASS NUCLEI
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550201* - Biochemistry- Tracer Techniques