Ultra-violet Absorption Spectra of Haemoglobins from Various Vertebrates

Abstract

IT is well known that the various vertebrate haemoglobins as well as the individual variants of adult human haemoglobin (Hb A) may be readily distinguished by their different mobility in electrophoresis, adsorbability and stability to thermal denaturation. A possibility of identification, particularly in abnormal haemoglobins, is offered by recombination analysis and, finally, by the determination of the amino-acid composition and sequence. We found the ultra-violet spectrum as recorded between 39,000 and 34,000 cm⁻¹ provided a very simple additional means of differentiation. Little information can be obtained from the literature^1,3,4. Hb F (foetal human haemoglobin) may be recognized from its well-distinguishable tryptophan band at 34,400 cm⁻¹, and Matsuda⁴ directed attention to the absorption differences between the human α-, β-and γ- chains. If the ultra-violet spectrum is recorded at high resolution using an appropriate haemoglobin derivate, however, many more differentiated results may be achieved.