L.C. PETCU*, G. TURCU**, NATALIA ROSOIU*

*Faculty of Medicine, „Ovidius” University, Constanţa, Romania
**Faculty of Physics, Bucharest University, Romania

Abstract. The purpose of this survey is to highlight certain aspects related to the structure-function relation that governs the existence of hemoglobin as an allosteric protein, using absorption and fluorescence spectroscopy techniques, and a number of substances known as allosteric effectors of hemoglobin. This paper presents a method of indirect fluorescence labeling of hemoglobin and its derivatives with 8-hydroxy-l,3,6 pyrentrisulfonic acid trisodium salt (HPT), a functional analogue of 2,3-biphosphoglycerate (BPG), possessing more favorable physical properties, considering that heme is a strong quencher of any fluorescent molecule that might he used for the direct labeling of hemoglobin. Fluorescence spectra were recorded for oxyhemoglohin labeled with HPT, methemoglohin labeled with HPT, cyanhemoglohin labeled with HPT and fluorhemoglobin labeled with HPT.

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