Solubilization and molecular weight estimation of prolactin receptors from Rana catesbeiana tadpole liver and tail fin.
Explore the source record for details and available documents.
Animals↗
Biomedical subjects
F E Carr
Publications and source records attributed to F E Carr.
Prolactin and tadpole metamorphosis. Evidence of prolactin receptors in premetamorphic Rana catesbeiana liver and tail fin.
The binding characteristics of ovine prolactin (OPRL) to a particulate fraction from liver and tail fin of Rana catesbeiana tadpoles were studied. The specific binding of [125I]oPRL to both tissues was found to be a saturable process with a single class of binding sites in each tissue. Although the dissociation constants were similar for each tissue, the tail fin demonstrated a 10-fold higher binding capacity than the liver tissue. Pretreatment of the liver and tail fin particulate fractions with degradative enzymes revealed that trypsin and phospholipase C reduced the subsequent specific [125I]oPRL binding in both tissues. However, neuraminidase treatment decreased the prolactin binding in the liver while having no effect on the tail fin. The binding of prolactin to the amphibian tissues was found to be specific for prolactin and growth hormones. [125I]oPRL binding to both tissues was a reversible process although the dissociation rate was faster for the tail fin than for the liver. Therefore, prolactin receptors are associated with both a prolactin responsive tissue, the tail, and an unresponsive tissue, the liver, in the tadpole.
Animals↗
Instructors' ratings of delinquents after outward bound survival training and their subsequent recidivism.
Explore the source record for details and available documents.
Adaptation, Psychological↗
Immunogenicity of a unique region of the human thyrotropin receptor.
Clarifying the role of the TSH receptor protein in the autoimmune process may be the key to understanding the development of Graves' disease. In the present study we used a 16 amino acid peptide of the human TSH receptor (hTSHR) to immunize rabbits. A comparable, but theoretically less immunogenic, peptide was injected into other rabbits. The antibody response against these and other peptides, as well as against solubilized human thyroid membrane (TM) and guinea pig fat cell membrane (GPF) proteins, was tested using ELISA and Western blots. The GPF and TM binding pattern of rabbits' sera was compared to that of Graves' patients' sera. We have identified an area of antigenic cross-reactivity between GPF and TM; a 63 kD protein was present in both GPF and TM, and this protein uniformly bound IgG-s of the rabbits' postimmunization sera and one of eight Graves' patient's serum. We have shown that i) a theoretically immunogenic 16 amino acid peptide was indeed highly immunogenic in rabbits, ii) antibodies binding to GPF and TM were detected after immunization, and iii) the peak of thyroid stimulating immunoglobulin activity of sera was followed by a transient elevation of serum triiodothyronine levels. Further studies investigating the immunogenic epitopes of the hTSHR as well as characterizing the 63 kD protein are indicated.
Amino Acid Sequence↗