Molecular cloning and chromosomal localization of human 4-beta-galactosyltransferase.
AUTOR(ES)
Humphreys-Beher, M G
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=387044Documentos Relacionados
- Molecular cloning and chromosomal localization of human 4β-galactosyltransferase
- Molecular cloning and chromosomal localization of one of the human glutamate receptor genes.
- Antidepressant- and cocaine-sensitive human serotonin transporter: molecular cloning, expression, and chromosomal localization.
- Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase.
- Molecular cloning and chromosomal localization of DNA sequences associated with a human DNA repair gene.
