Development of TaqMan PCR assay for detection of A and B variants of the bovine β-lactoglobulin

References

• Schaar J, Hansson B, Pettersson H. Effects of genetic variants of κ-casein and β-lactoglobulin on cheesemaking. J. Dairy Res. 1985;52(3):429–437.
   Web of Science ®Google Scholar
• Hallen E, Wedholm A, Andren A, Lunden A. Effect of beta-casein, kappa-casein and beta-lactoglobulin genotypes on concentration of milk protein variants. J Anim Breed Genet. 2008;125(2):119–129.
   PubMed Web of Science ®Google Scholar
• Huang W, Peñagaricano F, Ahmad KR, Lucey JA, Weigel KA, Khatib H. Association between milk protein gene variants and protein composition traits in dairy cattle. J Dairy Sci. 2012;95(1):440–449.
   PubMed Web of Science ®Google Scholar
• O’Mahony JA, Fox PF. Milk: an overview. In Singh H, Boland M, Thompson A, eds. Milk Proteins. 2nd ed. San Diego, CA: Academic Press; 2014: 19–73.
   Google Scholar
• Hambling SG, McAlpine AS, Sawyer L. β-lactoglobulin. In Fox PF, ed. Advanced Dairy Chemistry, Proteins 1. London: Elsevier Applied Science; 1992: 141–190.
   Google Scholar
• Creamer L, Parry D, Malcolm G. Secondary structure of β-lactoglobulin B. Arch Bioch Bioph. 1983;227(1):98–105.
   PubMed Web of Science ®Google Scholar
• Hill JP, Thresher WC, Boland MJ, et al. The polymorphism of the milk protein β-lactoglobulin. In:  Welch, et al., ed. Milk Composition, Production and Biotechnology. Wallingford, UK: CAB International; 1997: 173–213.
   Google Scholar
• Farrell HM, Jimenez-Flores R, Bleck GT, et al. Nomenclature of the proteins of cows' milk – sixth revision. J Dairy Sci. 2004;87(6):1641–1674.
   PubMed Web of Science ®Google Scholar
• Kontopidis G, Holt C, Sawyer L. Invited review: β-lactoglobulin: binding properties, structure, and function. J Dairy Sci. 2004;87(4):785–796.
   PubMed Web of Science ®Google Scholar
• Madureira AR, Pereira CI, Gomes AMP, Pintado ME, MalcataFX. Bovine whey proteins − overview on their main biological properties. Food Res Int. 2007;40(10):1197–1211.
   Web of Science ®Google Scholar
• Qin BY, Bewley MC, Creamer LK, Baker EN, Jameson GB. Functional implications of structural differences between variants A and B of bovinebeta-lactoglobulin. Protein Sci. 1999;8(1):75–83.
   PubMed Web of Science ®Google Scholar
• Harris S, Ali S, Anderson S, Archibald AL, Clark AJ. Complete nucleotide sequence of the genomicovine beta-lactoglobulin gene. Nucleic Acids Res. 1988;16(21):10379–10380.
   PubMed Web of Science ®Google Scholar
• Lemay DG, Lynn DJ, Martin WF, et al. The bovine lactation genome: Insights into the evolution of mammalian milk. Genome Biol. 2009;10(4):R43.
   PubMed Web of Science ®Google Scholar
• Casas E, Kehrli ME. A review of selected genes with known effects on performance and health of cattle. Front Vet Sci. 2016;3:113.
   PubMed Web of Science ®Google Scholar
• Badola S, Bhattacharya T, Biswas T, Kumar P, Sharma A. Association of beta-lactoglobulin polymorphism with milk production traits in cattle. Asian Australas J Anim Sci. 2003;16(11):1560–1564.
   Web of Science ®Google Scholar
• Miluchová M, Trakovická A, Gábor M. Analysis of beta-lactoglobuline gene (LGB) polymorphism in different breeds of bulls by high resolution melting. Sci Paper Anim Sci Biotechnol. 2012;45(1):193–197.
   Google Scholar
• Cecchinato A, Ribeca C, Maurmayr A, et al. Short communication: effects of β-lactoglobulin, stearoyl-coenzyme A desaturase 1, and sterol regulatory element binding protein gene allelic variants on milk production, composition, acidity, and coagulation properties of Brown Swiss cows. J Dairy Sci. 2012;95(1):450–454.
   PubMed Web of Science ®Google Scholar
• Kyselová J, Ječmínková K, Matějíčková J, et al. Physiochemical characteristics and fermentation ability of milk from Czech Fleckvieh cows are related to genetic polymorphisms of β-casein, κ-casein, and β-lactoglobulin. Asian-Australas J Anim Sci. 2019;32(1):14–22.
   PubMed Web of Science ®Google Scholar
• Medrano JF, Aguilar-Cordova E. Polymerase chain reaction amplification of bovine β-lactoglobulin genomic sequences and identification of genetic variants by RFLP analysis. Anim Biotechnol. 1990;1(1):73–77.
   Google Scholar
• Glazko VI, Andreichenko IN, Kovalchuk SN, Glazko TT, Kosovsky GY. Candidate genes for control of cattle milk production traits. Russ Agricult Sci. 2016;42(6):458–464.
   Google Scholar
• Schlee P, Rottmann O. Genotyping of bovine β‐casein, β‐lactoglobulin and α‐lactalbumin using the polymerase chain reaction. J Anim Breed Genet. 1992;109(1–6):456–464.
   Web of Science ®Google Scholar
• Kaminski S, Zabolewicz T. Genotyping of bovine beta-lactoglobulin (LBG) by PCR-SSCP technique. J Appl Genet. 1997;38(4):471–476.
   Google Scholar
• Maletić M, Aleksic N, Vejnovic B, Department of Reproduction, Fertility and Artificial Insemination, Faculty of Veterinary Medicine, University of Belgrade, Bul. oslobođenja 18, 11000 Belgrade, Serbia, et al. Polymorphism of κ-casein and β-lactoglobulin genes. Mljekarstvo. 2016;66(3):198–205.
   Web of Science ®Google Scholar
• Ardicli S, Samli H, Vatansever B, Soyudal B, Dincel D, Balci F. Comprehensive assessment of candidate genes associated with fattening performance in Holstein-Friesian bulls. Arch Anim Breed. 2019;62(1):9–32.
   PubMed Web of Science ®Google Scholar
• Jebin I, Das B, Borah P, Kalita DJ, Roy TC, Zaman GU. Genotyping of β-Lactoglobulin (β-Lg) gene by PCR-RFLP in indigenous cattle of Assam. India Indian J Anim Res. 2016;50(2):160–163.
   Google Scholar
• Herrmann MG, Durtschi JD, Bromley LK, Wittwer CT, Voelkerding KV. Amplicon DNA melting analysis for mutation scanning and genotyping: cross-platform comparison of instruments and dyes. Clin Chem. 2006;52(3):494–503.
   PubMed Web of Science ®Google Scholar
• Abdolmohammadi A, Atashi H, Zamani P, Bottema C. High resolution melting as an alternative method to genotype diacylglycerol O-acyltransferase 1 (DGAT1) K232A polymorphism in cattle. Czech J Anim Sci. 2011;56(8):370–376.
   Web of Science ®Google Scholar
• Seipp MT, Durtschi JD, Liew MA, et al. Unlabeled oligonucleotides as internal temperature controls for genotyping by amplicon melting. J Mol Diagn. 2007;9(3):284–289.
   PubMed Web of Science ®Google Scholar
• Krypuy M, Newnham GM, Thomas DM, Conron M, Dobrovic A. High resolution melting analysis for the rapid and sensitive detection of mutations in clinical samples: KRAS codon 12 and 13 mutations in non-small cell lung cancer. BMC Cancer. 2006;6(1):295.
   PubMedGoogle Scholar