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Recent studies have shown that ST6 beta-galactosamidealpha-2,6-sialyltransferase 1 (ST6GAL1), ST8alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4 (ST8SIA4),and solute carrier family 35, member C1 (SLC35C1) play essentialroles in the metabolism of milk glycoconjugates in mammals. However, studieson their coding genes in water buffalo have not been reported. In the presentstudy, cloning and sequencing showed that the coding sequences (CDSs) ofbuffalo ST6GAL1, ST8SIA4, and SLC35C1 were 1218,1080, and 1095 bp in length, which encoded a precursor protein composed of405, 359, and 364 amino acids, respectively. The deduced sequences of thesethree proteins in turn showed 97.6–98.5, 98.6–99.7, and 97.8–99.2 %similarities with other bovine species. Both buffalo ST6GAL1 andST8SIA4 were predicted to be a member of glycosyltransferase family29 and were all hydrophilicity proteins functioning in the Golgi apparatus.Buffalo SLC35C1 was a hydrophobic membrane protein located in theGolgi membrane, containing a TPT domain that is found in a number of sugarphosphate transporters. In addition, semi-quantitative RT-PCR analysis in 13lactating buffalo tissues revealed that the ST6GAL1 andST8SIA4 were expressed in 9 tissues, while SLC35C1 wasexpressed in 11 tissues. The expression levels of these three genes in themammary gland were significantly higher in lactating than in non-lactatingstage. Collectively, our data indicate that ST6GAL1,ST8SIA4, and SLC35C1 are potentially involved in the processof buffalo lactation

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Molecular cloning, sequence characterization, and tissue expression analysis of three water buffalo (&lt;i&gt;Bubalus bubalis&lt;/i&gt;) genes – &lt;i&gt;ST6GAL1&lt;/i&gt;, &lt;i&gt;ST8SIA4&lt;/i&gt;, and &lt;i&gt;SLC35C1&lt;/i&gt;