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Characterization of an equine alpha-S2-casein variant

ABSTRACT: Two major forms of equine αS2-casein arising from genomic 1.3 kb in-frame deletion involving two coding exons, one of which represents an equid specific duplication. Findings at the DNA-level have been verified by cDNA sequencing from horse milk of mares with different genotypes. At the protein-level, we were able to show by SDS-page and in-gel digestion with subsequent LC-MS analysis that both proteins are actually expressed

INSTRUMENT(S): Q Exactive

ORGANISM(S): Equus Caballus (horse)

SUBMITTER: Andreas Tholey

LAB HEAD: Andreas Tholey

PROVIDER: PXD002834 | Pride | 2018-10-17

REPOSITORIES: Pride

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			Action	DRS
	Maleika_1_1uL.msf-pride.pride.mgf.gz	Mgf
	Maleika_1_1uL.msf-pride.pride.mztab.gz	Mztab
	Maleika_1_1uL.msf-pride.xml.gz	Xml
	Maleika_1_1uL.raw	Raw
	Maleika_2_8uL.msf-pride.pride.mgf.gz	Mgf

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Publications

Characterization of an Equine α-S2-Casein Variant Due to a 1.3 kb Deletion Spanning Two Coding Exons.

Brinkmann Julia J Koudelka Tomas T Keppler Julia K JK Tholey Andreas A Schwarz Karin K Thaller Georg G Tetens Jens J

PloS one 20151007 10

The production and consumption of mare's milk in Europe has gained importance, mainly based on positive health effects and a lower allergenic potential as compared to cows' milk. The allergenicity of milk is to a certain extent affected by different genetic variants. In classical dairy species, much research has been conducted into the genetic variability of milk proteins, but the knowledge in horses is scarce. Here, we characterize two major forms of equine αS2-casein arising from genomic 1.3 k ...[more]

PMID: 26444874

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Analysis of casein alpha S1 & S2 proteins from different mammalian species.

Project description:Nowadays, the quality of any food used for human consumption is, to a considerable extent, considered by its possible contribution to the maintenance or improvement of the consumer's health. In developed countries there is increasing interest in goat milk and its derivates, the quality of which is considered of special importance in the light of current tendencies favouring healthy eating. In particular, goat's milk is a hypoallergenic alternative to cow's milk in the human diet. In the present work, we studied the casein alpha S1 and S2 proteins of cow, goat and sheep for comparative analysis. We found that the amino acid sequence of these proteins is almost same in goat and sheep but there are several changes at different base pairs when these two sequences are compared with cow. Prediction of secondary structures (GOR) was performed for alpha s1 and s2 proteins to gain functional insights. Our in silico study revealed considerable identity in chemical properties between goat and sheep but a considerable dissimilarity in cow with goat and sheep casein proteins. Moreover, the effect amino acid change on secondary structures in the three species is discussed. There was no significant difference found between goat and sheep alpha S1 and S2 proteins, so naturally both will be having same properties. The study concludes that sheep milk is another convenient alternative for the cow milk allergic children.

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