Mar 1, 1976

Quenching of tryptophanyl fluorescence of human growth hormone by iodide

Chemico-biological Interactions
V T Maddaiah, P J Collipp

Abstract

Quenching of tryptophanyl fluorescence of human growth hormone by I- followed saturation kinetics and was abolished by KSCN. In the presence of 6 M guanidine hydrochloride quenching was linear between 0 to 0.2 M KI. These results suggest that I- quenched the fluorescence of the native hormone by binding at or near the single tryptophanyl residue. Quenching by 0.1 M KI decreased exponentially with increasing concentrations of human and bovine growth hormones. Acidification did not have a significant effect on quenching of the human hormone, but it markedly decreased quenching of the bovine hormone. Conformational differences at the vicinity of the lone tryptophanyl residue that could be inferred by these and other experiments may be contributing to the biological specificity of native human and bovine growth hormones.

  • References5
  • Citations1

References

  • References5
  • Citations1

Citations

Mentioned in this Paper

Bos taurus
Acidification - ActCode
Fluorescence Spectroscopy
Plasma Protein Binding Capacity
Protein Conformation
Potassium thiocyanate
PMS-Tryptophan
Guanidine Hydrochloride
Growth hormone, bovine
Recombinant Growth Hormone

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