Abstract
Horses are unusual in producing protein-rich sweat for thermoregulation, a major component of which is latherin, a highly surface-active, non-glycosylated protein. The amino acid sequence of latherin, determined from cDNA analysis, is highly conserved across four geographically dispersed equid species (horse, zebra, onager, ass), and is similar to a family of proteins only found previously in the oral cavity and associated tissues of mammals. Latherin produces a significant reduction in water surface tension at low concentrations (=1 mg ml-1), and therefore probably acts as a wetting agent to facilitate evaporative cooling through a waterproofed pelt.
Original language | English |
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Article number | e5726 |
Number of pages | 12 |
Journal | PLoS ONE |
Volume | 4 |
Issue number | 5 |
DOIs | |
Publication status | Published - 29 May 2009 |
Keywords
- latherin
- equine physiology
- horses
- globular proteins
- sweat
- recombinant proteins
- surface tension
- fluorescence
- protein structure