Jan 1, 1976

Spectroscopic study of the structural changes of scorpion hemocyanin, induced by pH variations and addition of various salts

J J ToulméM Goyffon


Structural modifications of the scorpion haemocyanin induced by pH variations and salt addition are studied by U.V. absorption, fluorescence, circular dichroism and light scattering. Haemocyanin fluorescence is due to both aromatic amino-acids tyrosine and tryptophan. Deoxygenation or denaturation lead to a fourfold enhancement of its intensity. At acidic pH the active site is modified and the protein is dissociated, but at alkaline pH the haemocyanin aggregates. The addition of different salts (sodium citrate, potassium bromide and iodide...) involves protein dissociation, the amplitude of which depends on the anion. But pH variations and salt addition don't change the haemocyanin secondary structure as shown by circular dichroism. The C.D. spectrum of scorpion haemocyanin exhibits the characteristic bands of Arthropod haemocyanine.

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Mentioned in this Paper

Macromolecular Compounds
Fluorescence Spectroscopy
Bromides Measurement
Protein Conformation
Scorpio europaeus homeopathic preparations
Scorpion antigen
Spectrophotometry, Ultraviolet

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