Evaluation of ATP content in hair bulbs in human scalp.

The content of ATP in scalp hair bulbs in humans was measured in the hair roots from 15 healthy volunteers. Light and electron microscopy confirmed the presence of outer and an inner root sheaths in the root of pulled out anagen hair. Incubation of samples in buffer solution led to extraction of ATP, which was measured by the chemiluminescent method. Mechanic disintegration of hair bulbs and their freezing-defrosting did not increase ATP output. The results of microscopy indicated that ATP extraction procedure was associated with separation of the outer radical sheath from the inner one without impairing the structure of the inner sheath. The mean content of ATP was 12 ± 2 pmol per bulb. The use of pulled out hair bulbs for ATP measurements simplified the procedure as involved no surgical removal of follicles.

Photoinduced formation of thiols in human hair.

Raman, scanning electron, and optical microscopy of hair and spectrophotometry of soluble hair proteins are used to study the effect of UV-vis radiation on white hair. The samples of a healthy subject are irradiated using a mercury lamp and compared with non-irradiated (control) hair. The cuticle damage with partial exfoliation is revealed with the aid of SEM and optical microscopy of semifine sections. Gel filtration chromatography shows that the molecular weight of soluble proteins ranges from 5 to 7kDa. Absorption spectroscopy proves an increase in amount of thiols in a heavier fraction of the soluble proteins of irradiated samples under study. Raman data indicate a decrease in the amount of SS and CS bonds in cystines and an increase in the amount of SH bonds due to irradiation. Such changes are more pronounced in peripheral regions of hair. Conformational changes of hair keratins presumably related to the cleavage of disulfide bonds, follow from variations in amide I and low-frequency Raman bands. An increase in the content of thiols in proteins revealed by both photometric data on soluble proteins and Raman microspectroscopy of hair cuts can be used to develop a protocol of the analysis of photoinduced hair modification.

Effects of ultra violet radiation on the soluble proteins of human hair.

Exposure of hair fibers from healthy volunteers to Ultra Violet Radiation (UVR) under laboratory conditions enhanced protein elution from the hair tresses into a buffer solution (pH 10.5). At the same time the UVR decreased the intensity of tryptophan fluorescence in the eluted proteins. After mechanical homogenization of these hair samples, the increase of soluble protein was registered for UVR treated hair as well as the rise in sulfhydryl group content of these proteins. Analysis of soluble proteins from hair samples homogenized before and after protein elution has shown that mainly proteins rich in sulfhydryl groups were eluted and as a result sulfhydryl content of proteins in hair shaft decreased. The hypothesis concerning the effects of environmental factors on the properties of hair shaft proteins was examined, the proximal and distal parts of normal hair (0-5 cm and 15-20 cm from hair root) were compared. In the distal parts there was a higher quantity of soluble proteins registered after homogenization, with decreased sulfhydryl group content and tryptophan fluorescence. It could be supposed that this difference results from the steady rupture of cystine in sulfur bridges and tryptophan under exposure to environmental factors (mainly, UVR), followed by elution of the resulting peptides.