Molecular Characterization Of Hair Cuticle And Its Extracted Proteins In Seven Mammalian Species

Document Type : Original Article

Authors

Zoology Department, Faculty of Science, Mansoura University, Mansoura, Egypt.

Abstract

Hairisanoftheepidermisinmammalsandconsistsoftwolargegroupsofhumanhair proteins.Oneishardα-keratinsandtheotherismatrixproteins.Thepresentinvestigationaimed tocomparetheultrastructuralofthehairscaleusingthescanningelectronmicroscope,andthe proteinsandaminoacidscontentofthekeratininsevenmammalianspecies.
Thevaluesofthehairthickness,x/yferetandhairpatternofthespeciesinthepresent studyconfirmthepresenceofspecies-specificcharacteristicsandultrastructuralvariation.The situationinmandiffersfromthewildmammalsduetodamageofhaircuticlecausedby mechanicalabuse,exposuretoultravioletradiationandchemicaloverprocessing.The maximumamountofextractedproteinsfromhairkeratinwasanalyzedbySDS-PAGE.The electrophoreticpatternsshowedanoveralldegreeofsimilarity.However,differencesexist betweenspeciesintheintensityofstain.Quantitatively,theelectrophoreticpatternsscannedand analyzedusinggelproteinanalyzer.Theresultsshowednodifferencebetweenthemolecular massofsomespecies,butdifferentinmolecularmassdistribution.
Aminoacidcompositionofkeratinofmammalianhairspeciesofthepresentstudy showedsomevariation,especiallyformethionine,isoleucine,lysineandarginine.Theother aminoacidsstudiedaresignificantlypresentinmosthair.Oneofthelateraminoacidis




cysteine.Cysteineisaveryimportantdueto hepresenceofdisulfatecross-links.