ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Inhibition of the yeast-mycelial transition and the phorogenesis of Mucorales by diamino butanone (1988)
    Springer
    Archives of microbiology 151 (1988), S. 10-14 
    Details
    ISSN: 1432-072X
    Keywords: Mucor ; Phycomyces ; Diaminobutanone ; Polyamines ; Dimorphism ; Phorogenesis ; Ornithine decarboxylase ; Fungal differentiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Diamino butanone (DAB), a competitive inhibitor of ornithine decarboxylase (ODC) a key enzyme in polyamine biosynthesis, inhibited the yeast to hyphae transition in Mucor rouxii, induced by transfer from anaerobiosis to aerobiosis, but not the opposite phenomenon. Addition of DAB to anaerobic yeast cells brought about a decrease in ODC and polyamine levels. In these conditions, the aerobic shift produced only a weak increase in ODC activity and no change in polyamine levels. DAB also blocked phorogenesis in M. rouxii and in Phycomyces blakesleeanus. At the effective concentrations DAB did not affect cell growth of either fungus. It is suggested that low, constant levels of ODC and polyamines are necessary for cell growth, and that high transient levels are required during the differentiative steps. DAB, at the concentrations used, affects this last process, but does not interfere with the maintenance level of polyamines.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00444661
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Expression of Tn5-derived kanamycin resistance in the fungus Phycomyces blakesleeanus (1988)
    Springer
    Molecular genetics and genomics 212 (1988), S. 375-377 
    Details
    ISSN: 1617-4623
    Keywords: Phycomyces ; Transposon Tn5 ; Kanamycin ; Fungal transformation ; Fungal promoters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A plasmid, carrying the Tn5 gene for kanamycin resistance lacking its own promoter, has successfully been used in the selection of DNA sequences of the fungus Phycomyces blakesleeanus having promoter activity in Escherichia coli. Many of these sequences were also effective in promoting resistance to kanamycin when the corresponding chimeric plasmids were introduced in the fungus via spheroplast transformation. The selected phenotype was easily propagated through vegetative spores and behaved as a stable character since it was not appreciably lost in the absence of selection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334710
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Alterations in the vesicular pattern and wall growth ofPhycomyces induced by the calcium ionophore A 23187 (1989)
    Springer
    Protoplasma 148 (1989), S. 15-25 
    Details
    ISSN: 1615-6102
    Keywords: Vesicles ; Phycomyces ; Calcium ionophore ; Chitin synthetase ; Invertase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Hyphal elongation, chitin synthesis in vivo, and invertase secretion inPhycomyces blakesleeanus were all inhibited almost instantly by the addition of 5–10 μM calcium ionophore A 23187. Protein biosynthesis was inhibited in these conditions by 30–50%. The ionophore did not affect cell respiration for at least 40 min. Effect on chitin biosynthesis was not due to alterations of the chitin synthetase levels or its activity; nor to impairement in GlcNAc metabolism. In drug-treated cells the number of apical vesicles was severely reduced even at very short periods of incubation, and these low numbers remained constant for at least 60 min of incubation with the ionophore. We suggest that the ionophore collapses the cellular calcium gradient and/or interferes with the normal electrical transhyphal current. As a consequence, formation and migration of apical vesicles are inhibited. These results are further evidence of the role of vesicles in fungal tip growth and exhibit the fact that active chitin synthetase is short-lived in vivo demanding its continuous supply by chitosomes to the cell surface.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01403987
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    facet.materialart.
    Unknown
    Physiological constraint on feeding behavior: intestinal membrane disaccharidases of the starling (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-10
    Description: Animals clearly choose what they eat and can even choose among chemically different sugars. The physiological and biochemical mechanisms that constrain feeding choices are largely unknown. In this study, European starlings (Sturnus vulgaris) preferred mixture solutions of D-glucose plus D-fructose to equimolar (double molar caloric value) solutions of sucrose. Intubation feeding of sucrose did not increase blood glucose levels. Sucrose is a useless energy source for these birds because they lack a single digestive enzyme (sucrase) on the small intestinal brush border membrane. However, the membranes possessed separate maltase and isomaltase disaccharidases. This expression pattern and expression patterns of membrane disaccharidases among mammals suggest a role for intestinal enzymes in the coevolutionary interactions between vertebrates and their plant food sources.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez del Rio, C -- Stevens, B R -- DK-38715/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 10;243(4892):794-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Florida, Gainesville 32611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2916126" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Birds/*physiology ; Disaccharidases/physiology ; Disaccharides/metabolism ; Feeding Behavior/*physiology ; Intestinal Mucosa/enzymology ; Intestines/*physiology ; Microvilli/enzymology ; Sucrase/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Neuronal pp60c-src contains a six-amino acid insertion relative to its non-neuronal counterpart (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-24
    Description: Neuronal cells express a pp60c-src variant that displays an altered electrophoretic mobility and a different V8 peptide pattern relative to pp60c-src expressed in tissues of non-neuronal origin. To determine whether the neuronal form of pp60c-src is encoded by a brain-specific messenger RNA, a mouse brain complementary DNA (cDNA) library was screened with a chicken c-src probe and a 3.8-kilobase c-src cDNA clone was isolated. This clone encodes a 60-kilodalton protein that differs from chicken or human pp60c-src primarily in having six extra amino acids (Arg-Lys-Val-Asp-Val-Arg) within the NH2-terminal 16 kilodaltons of the molecule. S1 nuclease protection analysis confirmed that brain c-src RNA contains an 18-nucleotide insertion at the position of the extra six amino acids. This insertion occurs at a position that corresponds to a splice junction in the chicken and human c-src genes. The isolated c-src cDNA clone encodes a protein that displays an identical V8 peptide pattern to that observed in pp60c-src isolated from tissues of neuronal origin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez, R -- Mathey-Prevot, B -- Bernards, A -- Baltimore, D -- P0I CA38497/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):411-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2440106" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/enzymology ; Chickens ; Cloning, Molecular ; DNA/metabolism ; DNA Restriction Enzymes ; DNA Transposable Elements ; Humans ; Isoenzymes/*genetics ; Mice ; Neurons/*enzymology ; Protein Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins pp60(c-src) ; Sequence Homology, Nucleic Acid ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...