KERATIN STRUCTURAL ORGANISATION OF NORMAL AND PATHOLOGICAL THINNED WOOL FIBERS
V. V. Havrylyak1, H. M. Sedilo2
This email address is being protected from spambots. You need JavaScript enabled to view it.
1Institute of Animal Biology NAAS, V. Stus str., 38, Lviv 79034, Ukraine
2Institute of Agriculture of Carpathian region NAAS, Hrushevskoho str., Obroshyno village,
Lviv region, 81115, Ukraine
The method of wool fiber extraction that allows quantifies four protein fractions has been described in the paper.
For analysis normal and pathologically thinned wool fibers of Askanian crossbred ewes were used.
Using a combination of reducing agent with different concentration and anionic detergent matrix protein, microfibrils protein, high molecular mass protein and cuticle residue were isolated from wool fibers.
Obtained proteins were analyzed by SDS-electrophoresis. The protein fraction was composed of microfibril keratins with molecular mass of 40–50 kDa, matrix or keratin-associated protein with a molecular mass of 10–30 kDa and high molecular mass minor protein component (100 kDa). These data indicate that the electrophoretic profile of wool fiber keratin consistent with its structural components, obtained by extraction.
The correlation of different protein components in the normal and pathological thinned wool fibers was investigated. It was shown that such defect wool fiber as a thinning characterized by decrease of matrix or keratin-associated proteins, indicating a redistribution of the crystalline and amorphous phases in the fiber.
This method can be applied to analyze the structural changes of keratin fibers component damaged due different nutritional, physical or chemical factors.
Key words: WOOL FIBRE, KERATIN, FRACTIONING, MATRIX PROTEINS, MICROFIBRIL PROTEINS, HIGH MOLECULAR WEIGHT PROTEINS, CUTICLE
Download full text in PDF format
