PubMed · 13828151
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P GIRAUD, A ORSINI, G BOFFA. 1960. [Dyshemoglobinoses C, D and E].. https://pubmed.ncbi.nlm.nih.gov/13828151/
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BACKGROUND/AIMS: Although reflectance spectrophotometry is often applied to measurement of skin color, raw data of reflectance spectra of normal and lesional skin are difficult to analyze. The purpose of this pilot study was to determine whether measurement of spectral difference in absorbance (SDA) between various skin lesions and normal skin adjacent to them could yield useful information for clinics in dermatology. METHODS: We studied spectral reflectance of a total of 173 various skin lesions. After converting obtained reflectance into apparent absorbance A (=log(10)(1/reflectance)), we examined the profile of SDA, that is, A(lesion)-A(normal skin) in the range of 400-700 nm, and compared them with the absorbance spectra of melanin and hemoglobin. RESULTS: SDA of epidermal pigmentary disorders was similar to the absorption spectrum of melanin in vitro, but the cases with intradermal melanin deposition showed a different pattern, reflecting the scattering effect of the dermis. SDA of erythematous lesions was similar to the spectra of either oxygenated or reduced hemoglobin, and varied according to the oxygenated level of cutaneous blood. SDA of lesions with a combination of factors appeared as a simple summation of spectra corresponding to each of the factors. CONCLUSIONS: Our method may offer easy and quick detection of major pathophysiological changes in skin lesions.
In the absence of experimental methods for determining concentrations of species in protein-ligand binding, it is not possible to determine the thermodynamic properties of species directly. However, this article on a simple reaction system shows that measurements of the average number of oxygen molecules bound at various T, pH and concentrations of molecular oxygen can be used to calculate thermodynamic properties of species. The simple system considered has some of the characteristics of the binding of oxygen by hemoglobin, but it has been simplified so that the method for obtaining thermodynamic information can be clarified. A table of standard thermodynamic properties of species is the most efficient way to store thermodynamic information on a reaction system. All the standard further transformed thermodynamic properties at specified T, pH and concentrations of molecular oxygen, all the standard transformed thermodynamic properties at specified T and pH, and all the standard thermodynamic properties of species at a specified temperature can be calculated. These calculations are based on the fact that the mathematical function for the standard further transformed Gibbs energy of the system contains all the thermodynamic information on the system. These properties are all interrelated by Maxwell equations.
Functionally distinct conformations of HbA (human adult hemoglobin) were probed using deoxy and diliganded derivatives of symmetric Fe-Zn hybrids of HbA. To expand the range of accessible structures, different environments were utilized including solution, sol-gel encapsulation, and crystals. Further structural and functional modulation was achieved by the addition of allosteric effectors. Functional characterization included oxygen affinity measurements, CO combination rates, and geminate and bimolecular CO recombination, after photodissociation. The conformational properties were studied using visible resonance Raman spectroscopy as a probe of local tertiary structure at the iron-containing hemes and UV resonance Raman spectroscopy as a probe of elements of the globin known to be sensitive to quaternary structure. The combined results show a pattern in which there is a progression of conformational and functional properties that are consistent with a picture in which the T quaternary structure can accommodate a range of tertiary conformations (plasticity). At one end of the distribution is the equilibrium deoxy T state conformation that has the lowest ligand reactivity. At the other end of the distribution are T state conformations with higher ligand reactivity that exhibit "loosened" T state constraints within the globin including the alpha(1)beta(2) interface and reduced proximal strain at the heme.