The voluminous literature of the comparative aspects of oxygen-hemoglobin equilibrium has received several complete reviews (Redfield, '33 ; Florkin, '34 ; Prosser, '50). Krogh and Leitch ('19) reported that, in both fresh and salt water, species of fish which frequently encounter low oxygen tensio
A comparative study of hemoglobin denaturation
โ Scribed by Ramsey, Helen J.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1941
- Tongue
- English
- Weight
- 534 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0095-9898
No coin nor oath required. For personal study only.
โฆ Synopsis
When hemoglobin is exposed to alkali the globin portion of the molecule is altered resulting in the formation of globin hemochromogen. The rate at which such alkaline denaturation takes place is characteristic of the type of hemoglobin. I n 1934 Brinkman, Wildschut and Wittermans used specificity of denaturation rate to demonstrate the presence of two types of hemoglobin coexistent in human blood. Two
๐ SIMILAR VOLUMES
GuHCl denaturation profiles of 17 proteins were studied by the spectroscopic and chromatographic methods described in the preceding report. The profiles are broadly classified into three types according to their multiphasic characteristics. It seems likely that more complex processes than those prev
## FOUR FIGUKES Various extracellular annelid hemoglobins are very similar with regard to molecular weight, amino acid composition, solubility, and isoelectric point (reviewed : Lemberg and Legge, '49; Prosser, '50; Eliassen, ' 5 3 ) . It is reasonable to wonder if this similarity extends to other
Novel devices for the spectroscopic and chromatographic analysis of the denaturation curves of the protein are described. A multidimensional spectroscopic measuring system makes it possible to carry out simultaneous and continuous acquisition of a set of data of different spectroscopic dimensions at