| 1. |
- Bergström, S, et al.
(författare)
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Molecular characterization of Borrelia burgdorferi isolated from Ixodes ricinus in northern Sweden.
- 1992
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Ingår i: Scand J Infect Dis. - 0036-5548. ; 24:2, s. 181-8
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Tidskriftsartikel (refereegranskat)abstract
- Ixodes ricinus ticks, harbouring Borrelia burgdorferi, were found in an area in northern Sweden, not thought to be endemic for Lyme borreliosis. This investigation took place at Norrbyskär, an island situated in the Bothnian Gulf, 63 degrees 33'N/19 degrees 52'E. One of 42 nymphal and 8/43 adult I. ricinus ticks collected carried spirochetes as seen by phase contrast microscopy. Pure bacterial cultures were obtained from 2 of the ticks. Western blot analysis using species-specific monoclonal antibodies showed that the isolated spirochetes were B. burgdorferi. The identity of the isolated spirochetes was confirmed by DNA amplification using B. burgdorferi OspA and flagellin gene specific oligonucleotides as well as partial DNA sequencing of the respective OspA and flagellin genes. The 2 isolated spirochaete populations were different as shown by their protein profiles in sodium dodecyl sulphate polyacrylamide gels. Moreover, the demonstration of Lyme borreliosis in a patient from the island of Norrbyskär indicates the need for clinical consideration of this disease in northern Sweden.
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| 2. |
- Bergström, S, et al.
(författare)
-
Cloning and sequencing of human kappa-casein cDNA.
- 1992
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Ingår i: DNA Sequence. - 1042-5179. ; 3:4, s. 245-6
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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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| 3. |
- Hansson, L, et al.
(författare)
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Expression of human milk beta-casein in Escherichia coli : comparison of recombinant protein with native isoforms.
- 1993
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Ingår i: Protein Expression and Purification. - 1046-5928. ; 4:5, s. 373-81
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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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| 4. |
- Lönnerdal, Bo, et al.
(författare)
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Cloning and sequencing of a cDNA encoding human milk beta-casein.
- 1990
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Ingår i: FEBS Letters. - 0014-5793. ; 269:1, s. 153-6
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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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