The structure of two distinct pancreatic amylase genes in mouse strain YBR

Bm, Mikkelsen; Me, Clark; Christiansen, G.; Om, Klintebaek; Jt, Nielsen; Kk, Thomsen; Jp, Hjorth

doi:10.1007/bf00504287

Cited by 8 publications

(5 citation statements)

References 26 publications

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“…The low-stringency conditions used in the hybridization were as described previously . A single positive plaque was purified by replating on E. coli K802 and phage DNA was isolated from a 20 ml phage lysate (Mikkelsen et al, 1985).…”

Section: Methodsmentioning

confidence: 99%

Investigation of the translation-initiation factor IF2 gene, infB, as a tool to study the population structure of Streptococcus agalactiae The EMBL accession numbers for the sequences reported in this paper are AJ003164 and AJ251493 to AJ251499.

et al. 2000

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The sequence of infB, encoding the prokaryotic translation-initiation factor 2 (IF2), was determined in eight strains of Streptococcus agalactiae (group B streptococcus) and an alignment revealed limited intraspecies diversity within S. agalactiae. The amino acid sequence of IF2 from S. agalactiae and from related species were aligned and revealed an interspecies conserved central and C-terminal part, and an N-terminal part that is highly variable in length and amino acid sequence. The diversity and relationships in a collection of 58 genetically distinct strains of S. agalactiae were evaluated by comparing a partial sequence of infB. A total of six alleles were detected for the region of infB analysed. The alleles correlated with the separation of the same strains of S. agalactiae into major evolutionary lineages, as shown in previous work. The partial sequences of infB were furthermore used in phylogenetic analyses of species closely related to S. agalactiae, yielding an evolutionary tree which had a topology similar to a tree constructed using 16S rRNA sequences from the same species.

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Section: Methodsmentioning

confidence: 99%

Investigation of the translation-initiation factor IF2 gene, infB, as a tool to study the population structure of Streptococcus agalactiae The EMBL accession numbers for the sequences reported in this paper are AJ003164 and AJ251493 to AJ251499.

et al. 2000

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“…The low-stringency conditions used in the hybridization were as described above. Positive plaques were purified by replating on E. coli K802, and DNA was isolated from 20-ml phage cultures (24). PCR.…”

Section: Methodsmentioning

confidence: 99%

Characterization of the Streptococcus pneumoniae immunoglobulin A1 protease gene (iga) and its translation product

1996

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Bacterial immunoglobulin A1 (IgA1) proteases constitute a very heterogenous group of extracellular endopeptidases which specifically cleave human IgA1 in the hinge region. Here we report that the IgA1 protease gene, iga, of Streptococcus pneumoniae is homologous to that of Streptococcus sanguis. By using the S. sanguis iga gene as hybridization probe, the corresponding gene from a clinical isolate of S. pneumoniae was isolated in an Escherichia coli lambda phage library. A lysate of E. coli infected with hybridization-positive recombinant phages possessed IgA1-cleaving activity. The complete sequence of the S. pneumoniae iga gene was determined. An open reading frame with a strongly biased codon usage and having the potential of encoding a protein of 1,927 amino acids with a molecular mass of 215,023 Da was preceded by a potential ؊10 promoter sequence and a putative Shine-Dalgarno sequence. A putative signal peptide was found in the N-terminal end of the protein. The amino acid sequence similarity to the S. sanguis IgA1 protease indicated that the pneumococcal IgA1 protease is a Zn-metalloproteinase. The primary structures of the two streptococcal IgA1 proteases were quite different in the N-terminal parts, and both proteins contained repeat structures in this region. Using a novel assay for IgA1 protease activity upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we demonstrated that the secreted IgA1 protease was present in several different molecular forms ranging in size from approximately 135 to 220 kDa. In addition, interstrain differences in the sizes of the pneumococcal IgA1 proteases were detected. Southern blot analyses suggested that the S. pneumoniae iga gene is highly heterogenous within the species.

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“…The amylase complex on mouse chromosome 3 encodes both salivary and pancreatic amylase (Mikkelsen et al, 1985). On the other hand, at least two amylase genes are known in rats; Amy-l (in the pancreas) and Amy-2 (in the salivary gland), and only Amy-l was found to be polymorphic (Bender et al, 1984).…”

Section: Resultsmentioning

confidence: 99%

An electrophoretic polymorphism in salivary amylases (Amy-1) of mastomys (Praomys coucha)

Matsushima

Ikeno

et al. 1990

Lab Anim

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SummaryAn electrophoretic polymorphism of salivary amylases (Amy-I) in mastomys (Praomys coucha) (MWC, MRJ and MCC strains) was detected. Amylase in MWC or MRJ saliva, which migrated fast toward the anode, was designated as AMY-lA, and that in MCC saliva migrating slowly as AMY -lB. Salivary amylases are controlled by a pair of codominant alleles at a single autosomal locus (Amy-I). No polymorphism was seen in pancreatic amylases . The frequencies of these phenotypes did not differ between the sexes. Some isoamylases were observed and these were different from those in mouse or rat.

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The structure of two distinct pancreatic amylase genes in mouse strain YBR

Cited by 8 publications

References 26 publications

Investigation of the translation-initiation factor IF2 gene, infB, as a tool to study the population structure of Streptococcus agalactiae The EMBL accession numbers for the sequences reported in this paper are AJ003164 and AJ251493 to AJ251499.

Investigation of the translation-initiation factor IF2 gene, infB, as a tool to study the population structure of Streptococcus agalactiae The EMBL accession numbers for the sequences reported in this paper are AJ003164 and AJ251493 to AJ251499.

Characterization of the Streptococcus pneumoniae immunoglobulin A1 protease gene (iga) and its translation product

An electrophoretic polymorphism in salivary amylases (Amy-1) of mastomys (Praomys coucha)

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