Molecular cloning and chromosomal localization of human 4-beta-galactosyltransferase.
A cDNA clone to human 4-beta-galactosyltransferase (EC 2.4.1.38) was isolated from a human liver lambda gt11 expression library by using a monospecific polyclonal antiserum to affinity-purified bovine enzyme. The authenticity of this cDNA clone has been demonstrated by several criteria. Under conditions of chronic treatment with the beta-adrenergic receptor agonist isoproterenol, rat parotid glands show an approximately 10-fold increase in 4-beta-galactosyltransferase activity. The increased enzyme activity was reflected in dot-blot analysis of control and isoproterenol-treated rat parotid RNA by using the human cDNA as probe. Hybrid-selection and in vitro translation identified a protein product with a molecular mass of 47 kDa that was immunoprecipitated with the bovine antiserum. The full-length human cDNA clone was then isolated and the DNA sequence for the NH2-terminal portion of the protein was deduced. Comparison of the NH2-terminal protein sequence from the bovine protein with that of the human cDNA clone confirmed its identity. In addition, the human cDNA clone was used to localize the gene for 4-beta-galactosyltransferase to human chromosome 4 by Southern analysis of a somatic cell hybrid panel.
D000595:Amino Acid Sequence; D001483:Base Sequence; D002874:Chromosome Mapping; D002894:Chromosomes, Human, Pair 4; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005700:Galactosyltransferases / Q000235:genetics* / Q000276:immunology; D005786:Gene Expression Regulation / Q000187:drug effects; D006801:Humans; D007545:Isoproterenol / Q000494:pharmacology; D010306:Parotid Gland / Q000502:physiology; D012333:RNA, Messenger / Q000235:genetics
D012333:RNA, Messenger; D004247:DNA; D005700:Galactosyltransferases; D007545:Isoproterenol