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  • 1
    Electronic Resource
    Electronic Resource
    Human partoid size polymorphism (Ps): Characterization of two allelic products, Ps 1 and 2, by limited proteolysis (1983)
    Springer
    Biochemical genetics 21 (1983), S. 405-416 
    Details
    ISSN: 1573-4927
    Keywords: parotid size variant proteins ; human salivary proteins ; limited proteolysis ; isomorphic proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The allelically determined human salivary proteins, Ps 1 and 2, were purified on sodium dodecyl sulfate gels, eluted, and compared by limited proteolysis with Streptomyces griseus protease VI, Bacillus subtilis protease VII, and Staphylococcus aureus protease V8. Prior dansylation of the Ps isoproteins facilitated visualization of the peptides. Digestion patterns indicate considerable homology between the Ps isoproteins and support the conclusion [Azen, A. E., and Denniston, C. (1980). Biochem. Genet. 18:483] that there is an actual molecular weight difference between them. Further, the results suggest that this difference owes to an extension of the Ps 2 chain at one of its ends.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499148
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  • 2
    Electronic Resource
    Electronic Resource
    Human salivary proline-rich (Pr) proteins: A posttranslational derivation of the phenotypes (1979)
    Springer
    Biochemical genetics 17 (1979), S. 1061-1077 
    Details
    ISSN: 1573-4927
    Keywords: human saliva ; proline-rich proteins ; posttranslational modifications ; proteolytic cleavage ; isomorphic proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The acidic proline-rich proteins (Pr) showing genetic polymorphism were purified from human parotid salivas by gel filtration and ion exchange chromatography. Molecular weight determinations, amino acid composition analyses, and polypeptide mapping experiments indicate that the Pr 3 protein is a fragment of the Pr 1 protein. Studies of a parotid saliva factor capable of converting Pr 1 to Pr 3 and Pr 2 to Pr 4 indicate that Pr 3 and Pr 4 are generated from Pr 1 and Pr 2, respectively. Evidence suggests that the converting factor is a protease capable of posttranslationally cleaving Pr 1 and Pr 2, the primary or derived products of alleles Pr 1 and Pr 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504345
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  • 3
    Electronic Resource
    Electronic Resource
    Sex-limited effects of the expression of the db gene in mice during puberty (1981)
    Springer
    Biochemical genetics 19 (1981), S. 355-371 
    Details
    ISSN: 1573-4927
    Keywords: diabetic mice ; salivary proteins ; submandibular glands ; testosterone ; sex-limited expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The autosomal recessive gene diabetes (db) produces a condition similar to human insulin-dependent diabetes mellitus in certain strains of inbred mice. In this investigation, the effects of expression of the db gene on the development of the submandibular glands, electrophoretic protein patterns in salivas, fasting blood glucose levels, and glycosylated hemoglobin levels were evaluated in mice undergoing puberty. Three sex-limited effects of the db gene were observed in diabetic male mice: (1) a compromise of the development of the specialized submandibular glands with the extensive tubular portion normally found in males, (2) failure to develop a salivary protein pattern unique to male mice, and (3) attainment of higher levels of fasting blood glucose than found in female diabetic mice. Since it has been documented that homozygous mice fail to develop functional gonads, apparently due to insufficient production of gonadotropin, it is likely that the compromised development of the specialized submandibular glands, and, consequently, the male salivary protein pattern, is a result of decreased testosterone production. Experiments in which diabetic mice were treated with testosterone support that conclusion, since testosterone caused transformation of the salivary protein pattern to one identical with that of normal male littermate controls and increased the tubular portion of the submandibular glands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504280
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  • 4
    Electronic Resource
    Electronic Resource
    Sex-limited genetic variation in a mouse salivary protein (1982)
    Springer
    Biochemical genetics 20 (1982), S. 493-504 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484700
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  • 5
    Electronic Resource
    Electronic Resource
    Multiple gene action determining a mouse salivary protein phenotype: Identification of the structural gene for androgen binding protein (Abp) (1984)
    Springer
    Biochemical genetics 22 (1984), S. 657-667 
    Details
    ISSN: 1573-4927
    Keywords: androgen binding proteins ; mouse salivary proteins ; structural gene variation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A novel variation in electrophoretic phenotype is described for a mouse salivary androgen binding protein (Abp). Crosses show that the variation is inherited in an autosomal codominant manner and protein characterization studies show that the variant Abp differs in isoelectric point from the common form of the protein. Those observations suggest that the variation involves the structural gene for the mouse salivary Abp. The genetic studies also show that the electrophoretic mobility of the variant Abp can be influenced by the sex-limited saliva pattern (Ssp) gene. The Ssp S allele alters the electrophoretic mobility of Abp in males at puberty or in females which have received exogenous testosterone [Karn, R. C., Dlouhy, S. R., Springer, K. R., Hjorth, J. P., and Nielsen, J. T. (1982). Biochem Genet. 20:493]. This study shows that Abp and Ssp are distinct genes which are not closely linked and that Ssp S is trans active in F1 (Abp a /Abp b , Ssp S /Ssp F ) males.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485851
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  • 6
    Electronic Resource
    Electronic Resource
    Steroid Binding by Mouse Salivary Proteins (1998)
    Springer
    Biochemical genetics 36 (1998), S. 105-117 
    Details
    ISSN: 1573-4927
    Keywords: ANDROGEN-BINDING PROTEIN ; STEROID-BINDING ; SALIVARY PROTEINS ; SEXUAL SELECTION ; ASSORTATIVE MATE SELECTION BEHAVIOR ; PHEREMONE
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The goals of this study were to determine thesteroid-binding specificity of the mouse salivaryandrogen-binding protein (ABP) family and to ascertainwhether there might be other proteins in mouse saliva capable of binding steroids. The optimalconditions for testosterone binding by mouse salivaryproteins were determined using a small-scalechromatography system to separate bound from unboundsteroid. Testosterone binding appeared to be biphasicbut was directly proportional to saliva concentration,with an optimum temperature of 37 C in the second phase.These results were used to develop a steroid-binding protocol to study the steroid specificity ofsalivary proteins separated by electrophoresis. The ABPfamily bound testosterone and progesterone well andHO-progesterone and DHT to a lesser extent but did not bind either cholesterol or estradiol.Steroid structural comparisons suggest that binding byABP is governed by the A ring of the steroid. Anotherprotein that is not a member of the ABP family bound cholesterol specifically but no protein thatspecifically bound estradiol was observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018708404789
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  • 7
    Electronic Resource
    Electronic Resource
    A Comparison of the Structures of the Alpha:Beta and Alpha:Gamma Dimers of Mouse Salivary Androgen-Binding Protein (ABP) and Their Differential Steroid Bindin (1999)
    Springer
    Biochemical genetics 37 (1999), S. 187-199 
    Details
    ISSN: 1573-4927
    Keywords: SALIVARY ANDROGEN-BINDING PROTEIN ; STEROID BINDING ; DIMER STRUCTURE ; DIHYDROTESTOSTERONE ; TESTOSTERONE
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Mouse salivary androgen-binding protein (ABP) isa family of dimeric proteins that may play a pheromonalrole in Mus musculus. The protein dimer consists of acommon alpha subunit disulfide-bonded to avariable (beta or gamma) subunit. Here wereport N-terminal sequences of the beta and gammasubunits, showing that they are very similar to eachother while being quite different from the alphasubunit.We demonstrate differential androgen binding bythe two dimers. Both bind dihydrotestosterone to aboutthe same extent but the alpha:beta dimer bindssignificantly more testosterone than the alpha:gammadimer. We discuss the possible significance ofthis diversity of androgen binding with respect to thepossibility that androgen binding is related to aputative pheromonal role for the protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018786622052
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  • 8
    Electronic Resource
    Electronic Resource
    The amino acid sequence of the alpha subunit of mouse salivary androgen-binding protein (ABP), with a comparison to the partial sequence of the beta subunit and to other ligand-binding proteins (1993)
    Springer
    Biochemical genetics 31 (1993), S. 307-319 
    Details
    ISSN: 1573-4927
    Keywords: androgen-binding proteins ; microevolution ; mouse subspecies ; mouse salivary proteins ; pheromones
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract It has been suggested that three distinct genes,Abpa, Abpb, andAbpg, determine the three subunits of mouse salivary androgen-binding protein (ABP) (Dlouhy, S. R.,et al., Genetics 115, 535, 1987). We report the putative amino acid sequence of the subunit common to all forms of ABP, the Alpha subunit, and the partial amino acid sequence of the Beta subunit. These sequences have little in common, supporting the notion of at least two distinct genes coding for the subunits of the most common form of salivary ABP, the A:B dimer. A search of GenBank showed that these sequences have not been reported previously. The Beta subunit shows significant homology with helospectin, a member of the glucagon superfamily, but not enough homology to assign it to the family. No homology exists between ABP subunits and members of the ligand-binding carrier family of proteins nor does ABP show homology with other androgen-binding proteins. Particularly interesting is the observation that there is no relationship to rat prostatic steroid binding protein (PBP), given the similarities in protein tertiary structure, the numbers of subunits and their genes, and the earlier observation of ABP cross-reactive material in mouse prostate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553173
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  • 9
    Electronic Resource
    Electronic Resource
    Immunological relationships and a genetic interpretation of major and minor acidic proteins in human parotid saliva (1977)
    Springer
    Biochemical genetics 15 (1977), S. 549-562 
    Details
    ISSN: 1573-4927
    Keywords: human saliva ; proline-rich proteins ; isoelectric focusing ; phenotype ; immunological
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Isoelectric focusing was performed on parotid salivas selected for their electrophoretic phenotypes of proline-rich acidic salivary proteins. Fractions encompassing narrow pH regions were pooled and examined by polyacrylamide gel electrophoresis. Isoelectric focusing yielded partial purification of major and minor acidic proline-rich proteins which were subsequently compared by immunoelectrophoresis and double immunodiffusion against goat anti-human parotid saliva. Cross-reactivity without spurring between all fractions containing major Pr proteins in both immunoelectrophoresis and double immunodiffusion suggests that these proteins are immunologically very similar or identical.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00520197
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  • 10
    Electronic Resource
    Electronic Resource
    The tissue source and cellular control of the apparent size of androgen binding protein (Abp), a mouse salivary protein whose electrophoretic mobility is under the control of Sex-limited saliva pattern (Ssp) (1983)
    Springer
    Biochemical genetics 21 (1983), S. 1057-1070 
    Details
    ISSN: 1573-4927
    Keywords: mouse salivary protein ; heterodimeric structure ; androgen binding ; testicular feminization ; two-dimensional electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Expression of the dominant allele, Ssp Sat the Sex-limited saliva pattern locus in mice results in an alteration of the electrophoretic mobility of a mouse salivary protein from the F (fast) to the S (slow) type [Karn, R. C., et al. (1980). Genetics 94:s52; Karn, R. C., et al. (1982). Biochem. Genet. 20:493]. We now demonstrate that the protein affected binds androgen and has a basic heterodimeric structure with the subunits connected by disulfide bridging. It is produced in the submaxillary gland where the alteration takes place. The change in electrophoretic mobility from F to S appears to be primarily the result of an increase in the molecular weight of the larger subunit since the isoelectric point changes very little. We discuss the possible causes of the increase in molecular weight.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00488459
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