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  • 1
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] To address the problem of manure-based environmental pollution in the pork industry, we have developed the phytase transgenic pig. The saliva of these pigs contains the enzyme phytase, which allows the pigs to digest the phosphorus in phytate, the most abundant source of phosphorus in the pig diet. ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 13 (1975), S. 379-391 
    ISSN: 1573-4927
    Keywords: multiple hemoglobins ; Zoarces viviparus ; polypeptide chain ; genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Six major hemoglobin components are present in the teleostean fish Zoarces viviparus L. Biochemical characterization has led to a molecular model for the polypeptide chain composition of the individual hemoglobins. Only three different chains are involved. They are determined by three different structural loci, as indicated by the genetic variation of the electrophoretic hemoglobin pattern observed in natural populations. Hemoglobins occur that, despite identical chain compositions, have different electrophoretic mobilities. This may be due to a mechanism, known from man, where part of the hemoglobin is blocked by a hexose.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 17 (1979), S. 665-682 
    ISSN: 1573-4927
    Keywords: Mus musculus ; salivary amylase ; genetic variation ; rate of synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Heterozygotes from matings of the mouse strains YBR/Cv and C3H/As have about 3 times more YBR-amylase than C3H-amylase in the saliva. The determinant for this quantitative effect is located on linkage group XVI close to or within the structural gene for salivary amylase. The quantitative effect is the result of an increase in the rate of synthesis of YBR-amylase, and the determinant is cis acting. Studies of other mouse strains suggest that regulatory genetic elements may modulate salivary amylase production.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 18 (1980), S. 281-302 
    ISSN: 1573-4927
    Keywords: Mus musculus ; amylase ; structural genes ; peptide mapping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Salivary and pancreatic amylases from the mouse show both structural and quantitative genetic variation encoded within a gene complex on chromosome 3. Two fundamental questions prompted by this variation are whether salivary and pancreatic amylases are derived from different structural genes and whether multiple structural genes are causing the quantitative variation observed in each of the two amylases. These questions were approached by comparing the amylase protein from 12 congenic lines carrying amylase gene complexes derived from different origins. The amylases were purified by affinity chromatography employing the inhibitor cyclohepta-amylose and characterized in terms of amino acid composition, specific activity, molecular weight, and heat stability. They were analyzed by native electrophoresis in polyacrylamide gels and by peptide mapping employing both cyanogen bromide cleavage and restricted proteolysis in the presence of dodecylsulfate. By these techniques, many differences in the structure of pancreatic amylase that were not reflected in the salivary amylase were found among mouse strains. Likewise, a distinct salivary amylase variant was found. These results suggest that independent structural genes exist for the two amylases. Furthermore, by all criteria used, pancreatic amylase from single strains exhibits molecular heterogeneity, whereas heterogeneity was never found for salivary amylase. We conclude that at least four structural genes code for pancreatic amylase while only a single gene, different from any of the pancreatic genes, codes for salivary amylase.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 22 (1984), S. 257-273 
    ISSN: 1573-4927
    Keywords: amylase genes ; restriction patterns ; mouse genetic variation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The expression of pancreatic amylase in the mouse exhibits pronounced genetic variation. Congenic lines with various amylase complexes on a common C3H/As background have different numbers and forms of isoenzymes. The relative ratio of these isoenzymes may vary, as does the overall production of pancreatic amylase, which in some lines is three- to fourfold higher than in others. DNA from a number of lines was digested with endonucleases and hybridized to an amylase cDNA probe. The restriction patterns from inbred stocks and the corresponding congenic lines are identical, demonstrating that the majority of (if not all) amylase-like DNA sequences is found within the amylase complex. Congenic lines with specific amylase expression, for instance, in enzyme production, show different restriction patterns, whereas three lines with the same amylase phenotype have a uniform pattern. Most of the variation in amylase expression is represented among congenic lines derived from Danish mice. A comparison of such lines with others of remote geographic origin reveals that the restriction patterns of the “Danish” lines have by far the highest degree of resemblance. This observation seems to exclude major rearrangements within the amylase complex as the cause of the differences in enzyme expression, which instead are likely to be due to variation in regulatory elements associated with the active structural amylase genes in the complex.
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  • 6
    ISSN: 1573-4927
    Keywords: amylase genes ; DNA sequence ; mouse genomic λ-library ; pseudogenes ; restriction-heteroduplex maps
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The amylase complex on mouse chromosome 3 encodes both salivary and pancreatic amylase. It appears that one active gene is present for salivary amylase, whereas pancreatic amylase in some strains is coded by at least 4, and perhaps by more than 10, genes. Strain YBR is different from other strains in that it produces twice as much salivary amylase. Pancreatic amylase in YBR is present as two different protein forms, Aβ and Bβ, the sum of which amounts to only one-third of that in, for instance, strain A/J. YBR chromosomal DNA was cloned in phage λ, followed by restriction and heteroduplex analysis of recombinant phages carrying amylase genes. Among 32 phage isolates, 5 carried parts of the salivary amylase sequence. The remaining phage isolates contained pancreatic amylase-like sequences and represented three nonoverlapping genomic regions, i.e., one of 34 kb containing a complete gene, PAN-IIβ; another of 41 kb with a complete but different gene, PAN-Iβ, plus a truncated gene, PAN-ψ1; and finally, one of 23 kb with another truncated gene, PAN-ψ2. Parts of the amino acid sequence of Aβ and Bβ have previously been determined, and we report here the sequencing of a 4-kb DNA fragment from Pan-IIβ which establishes that this gene codes for Bβ.
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  • 7
    ISSN: 1573-4927
    Keywords: mouse salivary proteins ; electrophoresis ; testosterone ; sex-limited variation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract This report describes a gene which influences the electrophoretic mobility of a protein in the salivas of adult mice. Three categories of phenotype have been observed: the two single-banded types, F (Fast) and S (Slow), and the two-banded type, SF (Slow-Fast), with the two bands represented in varying proportions. All females, regardless of age or strain, and all males before puberty show only the F phenotype. Males of the BALB/c and C57BL/6J strains show the F phenotype throughout puberty and adult life, whereas males of the C3H/St and C57BL/KsJ strains show the SF phenotype in puberty and the S phenotype in adult life. We have designated this variation the sex-limited saliva pattern (Ssp). The results from genetic crosses indicate that the variation among the strains is determined by an autosomal locus, Ssp, with two alleles, Ssp S andSsp F ,where Ssp S is dominant to Ssp F .Testosterone treatment can accelerate the acquisition of the S type in males of the strains C3H/St and C57BL/KsJ and also induces that phenotype in C3H/St females and C57BL/6J males. Thus it appears that the observed strain-specific differences reflect a genetic variation in androgen levels and/or androgen sensitivity rather than variation in a structural gene.
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  • 8
    ISSN: 1573-9368
    Keywords: salivary ; parotid ; PSP ; enhancer ; murine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The murine PSP gene is expressed at a high-level in the parotid glands. To extend the knowledge of parotid gland expression and develop tools for expression of heterologous proteins in this tissue, the regulation of the PSP gene was studied using transgenic mice. High-level parotid gland expression of the PSP gene was indicated to depend on a novel regulatory region situated between −8.0 and −6.5 kb. Together with previous results this indicates that the main regulatory elements in the PSP gene are situated between −8.0 to −3.1 kb. This region was shown to activate a heterologous SV40 early promoter in the parotid glands of transgenic mice, suggesting that the PSP gene is controlled by enhancer sequences. A novel Psp derived 9.7 kb parotid gland expression cassette, Lama IV, carrying all known regulatory regions in the PSP gene was expressed at high-levels in the parotid glands and should prove highly useful for expression of heterologous proteins in the saliva of transgenic mice.
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  • 9
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 3 (1982), S. 1-6 
    ISSN: 0192-253X
    Keywords: glycerol-3-phosphate dehydrogenase ; isozymes ; mice ; genetics ; development ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Genetic variants that affect the heat stability and ionic charge of the adult isozyme of glycerol-3-phosphate dehydrogenase (EC 1.1.1.8) map to a gene, Gdc-1, located on chromosome 15. A second isozyme of glycerol-3-phosphate dehydrogenase, structurally homologous to the product of the Gdc-1 locus and expressed predominantly in undifferentiated tissues, has previously been identified. We have now discovered an electrophoretic variant of this embryonic isozyme. This expression is determined by a codominant allele of the gene, Gdc-2, that maps to the distal end of chromosome 9 as inferred from the observed gene order Mpi-1-d-Mod-1-Gdc-2.
    Additional Material: 1 Ill.
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  • 10
    Publication Date: 1982-02-01
    Print ISSN: 0018-067X
    Electronic ISSN: 1365-2540
    Topics: Biology
    Published by Springer Nature
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