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1997 | 38 | 4 |

Tytuł artykułu

Genotyping of bovine beta-lactoglobulin [LGB] by PCR-SSCP technique

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
A new method facilitating the identification of the two most common alleles (A and B) of the bovine beta-lacoglobulin (LGB) gene is described. The method is based on two steps: PCR amplification of 240 bp fragment of LGB gene followed by the single stranded conformation polymorphism (SSCP) detection. AA, AB and BB genotypes of LGB were identified with this technique. The PCR-SSCP is simple, accurate and relatively inexpensive. Additionally, this method has a potential to detect new variants within the amplified gene fragment.

Wydawca

-

Rocznik

Tom

38

Numer

4

Opis fizyczny

p.471-476,fig.

Twórcy

autor
  • Department of Animal Genetics, University of Agriculture and Technology, Oczapowskiego 5, 10-718 Olsztyn, Poland
autor
  • Department of Animal Genetics, University of Agriculture and Technology, Oczapowskiego 5, 10-718 Olsztyn, Poland

Bibliografia

  • Alexander L. J., Hayes G., Bawden W., Stewart A.F., Mackinlay A.G. (1993). Complete nucleotide sequence of the bovine β-lactoglobulin gene. Anim. Biotechnol. 4(1): 1-10.
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  • Bell K., Mckenzie H.A., Murphy W.H., Shaw D.C. (1970). β-lactoglobulin (Droughtmaster): A unique protein variant. Biochim. Biophys. Acta 214: 427-436.
  • Bell K., Mckenzie H.A., Shaw D.C. (1981). Bovine β-lactoglobulin E, F and G of Bali (Banteng) cattle, Bos (Bibos) javanicus. Aust. J. Biol. Sci. 34: 133-147.
  • Braunitzer G., Chen R., Schrank B., Stangl A. (1973). Die Sequenzanalyse des β-lactoglobulins. Z. Physiol. Chem. 354: 867-878.
  • Brignon G., Ribadeau-Dumas B. (1973). Localisation dans la chaine peptidique de la β-lactoglobulinc bovine dc la substitution Glu/Gln differenciat les variants génétiques В et D. FEBS Lett. 33: 73-76.
  • Conti A., Napolitano L.,Cantisani A. M., Davoli R., Dall'Olio S. (1988). Bovine beta-lactoglobulin H: isolation by preparative isoelectric focusing in immobilized pH gradients and preliminary characterization. J. Biochcm. Biophys. Methods 16: 205-214.
  • Eggen A., Fries R. (1995). An integrated cytogenetic and meiotic map of the bovine genome. Anim. Genet. 26: 215-236.
  • Fox P.F. (1992). Advanced Dairy Chemistry. Volume 1. Proteins. Elsevier Science Publishers Ltd., London & New York.
  • Frutos de M., Molina E., Amigo L. (1996). Applicability of capillary electrophoresis to the study of β-lactoglobulin polymorphism. Milchwissenschaft 51(7): 374-376.
  • Godovac-Zimmermann J., Krause I., Buchberger J., Weiss G., Klostermeyer H. (1990). A novel wild-type β-lactoglobulin W and its primary sequence. Biol. Chem. Hoppe-Seyeer 371: 255-260.
  • Hayes H.C., Petit E.J. (1993). Mapping of the β-lactoglobulin gene and of an immunoglobulin M heavy chain-like sequence to homologous cattle, sheep and goat chromosomes. Mamm. Genome 4(4): 207-210.
  • Jakob E„., Puhan Z. (1992). Technological properties of milk as influenced by genetic polymorphism of milk proteins (a review). Inter. Dairy J. 2: 157-178.
  • Jamieson A.C., Vandeyar M.A., Kang Y.C., Kinsella J.E., Bait C.A. (1987). Cloning and nucleotide sequence of bovine β-lactoglobulin gene. Gene 61: 85-90.
  • Li C.H. (1946). Electrophoretic inhomogeneity of crystalline β-lactoglobulin. J. Amer. Chem. Soc. 68: 2746-2747.
  • Мао I. L., Bittazzoni L. G., Aleandri R. (1992). Effects of polymorphic milk protein genes on milk yield and composition traits in Holstein cattle. Acta Agricul. Scand. S. A: Anim. Sci. 42: 1-8.
  • Medrano J.F., Aguilar-Cordova E. (1990). Polymerase chain reaction amplification of bovine β-lactoglobulin genomic sequences and identification of genetic variants by RFLP analysis. Anim. Biotechnol. 1: 73-77.
  • Michalak W. (1967). Anomalous electrophoretic pattern of milk proteins. J. Dairy Sci. 50: 1319-1325.
  • Orita M., Iwahara H., Kanazawa H., Hayashi K., Sekiya T. (1989). Detections of polymorphisms of human DNA by gel electrophoresis as single-strand conformation polymorphisms. Proc. Nat. Acad. Sci. USA 86: 2766-2770.
  • Pervaiz S., Brew K. (1985). Homology of β-lactoglobulin, scrum retinol binding protein, and protein HC. Science 228: 335-337.
  • Polis P.D., Schmucker H.W., Custer J.H., Mcmeekin T.L. (1950). Isolation of an electrophoretically homogeneous crystalline component of β-lactoglobulin. J. Amer. Chem. Soc. 72: 4965-4968.
  • Seibert BB., Erhardt G., Senft B. (1985). Procedure for simultaneous phenotyping of genetic variants in cow’s milk by isoelectric focusing. Anim. Blood Groups Bioch. Genet. 16: 183-191.
  • Sheffield V.C., Beck J.S., Kwitek A.E., Sandstrom D.W., Stone E.M. (1993). The sensitivity of single-strand conformation polymorphism analysis for the detection of single base substitutions. Genomics 16: 325-332.
  • Tadashi H., Buzard G. S., Calvert L.J., Weghorst C.M. (1993). "Cold SSCP": a simple, rapid and non-radioactive method for optimized single-strand conformation polymorphism analyses. Nucleic Acids Res. 21, 16: 3637-3642.
  • Tee M.K., Moran C., Nicholas F.W., Mackinlay A.G. (1991). The electrophoretic difference between the A and В variants of cattle β-lactoglobulin corresponds to an Hph I RFLP in exon III. Anim. Biotcchnol. 2(1): 31-43.
  • Wagner V.A., Schild T. A., Geldermann H. (1994). DNA variants within the 5-flanking region of milk-protcin-encoding genes. II. The β-lactoglobulin-cncoding gene. Theor. Appl. Genet. 89: 121-126.
  • Willis I.M., Stewart A.F. Caputo A., Thompson A.R., Mackinlay A.G. (1982). Construction and identification by partial nucleotide sequence analysis of bovine casein and β-lactoglobulin cDNA clones. DNA 1: 375-386.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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