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Sökning: swepub > Umeå universitet > Tidskriftsartikel > (1990-1994) > Bergström S

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1.
  • Bergström, S, et al. (författare)
  • Cloning and sequencing of human kappa-casein cDNA.
  • 1992
  • Ingår i: DNA Sequence. - 1042-5179. ; 3:4, s. 245-6
  • Tidskriftsartikel (refereegranskat)abstract
    • A cDNA encoding kappa-casein of human milk was cloned and sequenced. The kappa-casein cDNA was isolated from a lambda gt11 library generated from mRNA prepared from a mammary gland biopsy obtained from a lactating woman. The library was screened with polyclonal rabbit antibodies raised against purified native kappa-casein. The obtained nucleotide sequence contained an ORF sufficient to encode the entire amino acid sequence of a kappa-casein precursor protein consisting of 182 amino acids. This includes a tentative signal peptide of 20 amino acids and a processed protein of 162 amino acids.
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2.
  • Hansson, L, et al. (författare)
  • Expression of human milk beta-casein in Escherichia coli : comparison of recombinant protein with native isoforms.
  • 1993
  • Ingår i: Protein Expression and Purification. - 1046-5928. ; 4:5, s. 373-81
  • Tidskriftsartikel (refereegranskat)abstract
    • Studies on physiological function and on structure-function relationships of human milk beta-casein have been limited. In this study, we have introduced the human beta-casein cDNA into vectors designed for expression in Escherichia coli. The inducible T7-based expression system resulted in high-level expression of recombinant beta-casein. The recombinant beta-casein, localized intracellularly in E. coli, was purified to homogeneity and compared with purified native beta-casein, in particular with respect to phosphorylation. The E. coli-produced beta-casein was found to comigrate with the full-length, nonphosphorylated native human beta-casein isoform on SDS-PAGE. An N-terminal peptide containing all tentative phosphorylation sites was isolated from the recombinant protein and analyzed by mass spectrometry. The molecular mass as well as the migration of this peptide on reversed-phase chromatography confirmed that it was unphosphorylated.
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3.
  • Jonsson, Maria, et al. (författare)
  • Heterogeneity of outer membrane proteins in Borrelia burgdorferi : comparison of osp operons of three isolates of different geographic origins.
  • 1992
  • Ingår i: Infection and Immunity. - American Society for Microbiology. - 0019-9567. ; 60:5, s. 1845-53
  • Tidskriftsartikel (refereegranskat)abstract
    • Biochemical and immunochemical studies of the outer membrane proteins of Borrelia burgdorferi have shown that the OspA and OspB proteins from strains of different geographic origins may differ considerably in their reactivities with monoclonal antibodies and in their apparent molecular weights. To further characterize this variation in Osp proteins between strains, the osp operons and deduced translation products from two strains, one from Sweden (ACAI) and one from eastern Russia (Ip90), were studied. Polyacrylamide gel electrophoresis and Western blot (immunoblot) analyses confirmed differences between ACAI, Ip90, and the North American strain B31 in their Osp proteins. The sequences of the ospA and ospB genes of ACAI and Ip90 were compared with that of the previously studied osp operon of B31 (S. Bergström, V. G. Bundoc, and A. G. Barbour, Mol. Microbiol. 3:479-486, 1989). The osp genes of ACAI and Ip90, like the corresponding genes of B31, were found on plasmids with apparent sizes of about 50 kb and are cotranscribed as a single unit. Pairwise comparisons of the nucleotide sequences revealed that the ospA genes of ACAI and Ip90 were 85 and 86% identical, respectively, to the ospA gene of strain B31 and 86% identical to each other. The ospB sequences of these two strains were 79% identical to the ospB gene of B31 and 81% identical to each other. There was significantly greater similarity between the ospA genes of the three different strains than there was between the ospA and ospB genes within each strain. These studies suggest that the duplication of osp genes in B. burgdorferi occurred before the geographical dispersion of strains represented by ACAI, Ip90, and B31.
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4.
  • Lönnerdal, Bo, et al. (författare)
  • Cloning and sequencing of a cDNA encoding human milk beta-casein.
  • 1990
  • Ingår i: FEBS Letters. - 0014-5793. ; 269:1, s. 153-6
  • Tidskriftsartikel (refereegranskat)abstract
    • A cDNA of 1065 bp encoding the human milk beta-casein was cloned and sequenced using a synthetic oligodeoxyribonucleotide probe and a human mammary gland library. The nucleotide (nt) sequence contained an open reading frame sufficient to encode the entire amino-acid (aa) sequence of a beta-casein precursor protein consisting of 210 aa and a signal peptide of 15 aa. The nt sequence shows 45-62% homology to those of bovine, ovine, rat, and mouse beta-caseins. The highly phosphorylated site, which is responsible for the calcium-binding capacity of beta-casein, the signal peptide, and a sequence encoding for an inhibitor to the angiotensin-converting enzyme seem highly conserved among the beta-caseins with known sequences.
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Hernell, Olle (3)
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Strömqvist, M (2)
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