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  • 1
    Electronic Resource
    Electronic Resource
    Lactate dehydrogenase in preimplantation rabbit embryos (1975)
    Springer
    Biochemical genetics 13 (1975), S. 663-671 
    Details
    ISSN: 1573-4927
    Keywords: lactate dehydrogenase ; isoenzymes ; differentiation ; blastocyst ; gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Unfertilized eggs and early embryos up to the 2-day (16-cell) cleavage stage of development in the rabbit contain predominantly the most cathodal lactate dehydrogenase isoenzyme made up of A-type subunits. Following early cleavage there is a progressive increase in total LDH activity in the embryo as development proceeds through 4- and 6-day blastocyst stages. This is accompanied by an increase in the amounts of B-type subunits and a concomitant shift in the lactate dehydrogenase isoenzyme electrophoretic pattern toward the anodal isoenzyme types.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484924
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Lactate dehydrogenase in one-cell rabbit embryos extracted with triton X-100 (1976)
    Springer
    Biochemical genetics 14 (1976), S. 523-525 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486132
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Aldehyde oxidase cross-reacting material in the Aldox n, cin, mal, and lxd mutants of Drosophila melanogaster (1982)
    Springer
    Biochemical genetics 20 (1982), S. 111-124 
    Details
    ISSN: 1573-4927
    Keywords: immunoelectrophoresis ; insect hemolymph ; structural genes ; postsynthetic regulation ; genetic regulation ; enzymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Rocket immunoelectrophoresis was used to estimate aldehyde oxidase cross-reacting material (AO-CRM) in larval hemolymph and adult fly extracts in mutants with reduced AO enzymatic activity. Hemolymph of larvae homozygous for Aldox n, which is a mutation of the presumed structural gene for AO, contains 30% of the wild-type CRM. The demonstration of AO-CRM in Aldox n larval hemolymph is surprising since this genotype has been reported to lack CRM. By contrast, adult Aldox n flies lack detectable CRM. The other AO-deficient mutants that were examined are cin, mal, and lxd; each has appreciable levels of CRM in both larval hemolymph and adult extracts. Detection of CRM in these mutants helps to clarify conflicting reports in the literature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484940
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Xanthine dehydrogenase (XDH) cross-reacting material in mutants of Drosophila melanogaster deficient in XDH activity (1982)
    Springer
    Biochemical genetics 20 (1982), S. 125-132 
    Details
    ISSN: 1573-4927
    Keywords: immunoelectrophoresis ; postsynthetic regulation ; genetic regulation ; enzymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Rocket immunoelectrophoresis was used to estimate xanthine dehydrogenase cross-reacting material (XDH-CRM) in strains containing the cin 1 and cin 9 mutant genes, which are deficient in XDH enzymatic activity. CRM levels were determined as percentages of CRM in the Oregon-R wild-type strain. The mutant strains contain 72 and 76% of Oregon-R CRM, respectively. CRM levels in strains containing the XDH-deficient mutant genes lxd and mal are 93 and 105%, respectively. The high levels of CRM in these four mutant strains indicate that the primary effects of the mutant genes are on the function of XDH protein rather than its accumulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484941
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Fine structure of the pterin layer in the dermis of Rana pipiens (1971)
    Springer
    Cell & tissue research 113 (1971), S. 558-563 
    Details
    ISSN: 1432-0878
    Keywords: Pterin layer ; Pigmentation ; Dermis ; Development ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The fine structure of the pterin layer was investigated in both wild type Rana pipiens and Rana pipiens homozygous for the speckle mutant gene. No difference in morphology of the layer was noted between the wild type and mutant. The layer lines the outer surface of the stratum compactum of the dermis and separates this stratum from the stratum spongiosum. The pterin layer consists of extra-cellular material and contains membrane-bounded granules filled with fine spicules. Many of the spicules are somewhat similar in appearance to the initial calcification loci present in developing membrane bone. The layer first appears in the tadpole at approximately stage 14 (Taylor and Kollros, 1946); subsequent developmental stages are described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00325673
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    Paper (German National Licenses)
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