Jul 1, 1975

Acid-alkaline equilibrium of the ferri-leg-hemoglobin of the lupine (Lupinus luteus L.) Spectral studies

Molekuliarnaia biologiia
B P Atanasov, G Ia Zhizheskaia


Influence of pH was studied on the absorption spectra (340-670 nm) and on the curves of abnormal dispersion of optic rotation (220-270 nm) of the lupine ferri-leg-hemoglobin (Lb). pH range of the existence of the lupine Lb native form was determined (pH 5.5-11.0 at 20-25degrees C). It has been shown that not only met-hydroxy transition (which is in a complicated manner connected with the ionization of both ligand-bound water and certain amino acid residues of globin) but the ionization of a group with pK approximately 5, too, in the native molecule produces a heterotropic effect onto the haem. Complex analysis of the acidic and alkaline denaturation evidences that these processes are cooperative and proceed via several stages. pK values and the number of tyrosine residues were determined; it has been shown that these amino acid moieties are "buried" in the protein molecule. The results are discussed on the basis of a tentative model of the lupine Lb spatial suggested by the authors.

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Mentioned in this Paper

Lupinus luteus
Plasma Protein Binding Capacity
Hemoglobin Measurement
Protein Conformation
Spectrophotometry, Ultraviolet

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