ArticleBiomolecular NMR assignments2014
Resonance assignments for latherin, a natural surfactant protein from horse sweat.
Article in Biomolecular NMR assignments, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 3 citations in OpenAlex.
- Article
- Tandem Mass Tag (TMT) Proteomic Analysis of Saliva in Horses with Acute Abdominal Disease.Animals : an open access journal from MDPI · 2021Article
- Levels of horse allergen Equ c 4 in dander and saliva from ten horse breeds.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019Article
- The structure of latherin, a surfactant allergen protein from horse sweat and saliva.Journal of the Royal Society, Interface · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Latherin is an intrinsically surfactant protein of ~23 kDa found in the sweat and saliva of horses. Its function is probably to enhance the translocation of sweat water from the skin to the surface of the pelt for evaporative cooling. Its role in saliva may be to enhance the wetting, softening and maceration of the dry, fibrous food for which equines are adapted. Latherin is unusual in its relatively high content of aliphatic amino acids (~25% leucines) that might contribute to its surfactant properties. Latherin is related to the palate, lung, and nasal epithelium carcinoma-associated proteins (PLUNCs) of mammals, at least one of which is now known to exhibit similar surfactant activity to latherin. No structures of any PLUNC protein are currently available. (15)N,(13)C-labelled recombinant latherin was produced in Escherichia coli, and essentially all of the resonances were assigned despite the signal overlap due to the preponderance of leucines. The most notable exceptions include a number of residues located in an apparently dynamic loop region between residues 145 and 154. The assignments have been deposited with BMRB accession number 19067.
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