ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
    ISSN: 1432-072X
    Keywords: Saccharomyces cerevisiae ; Yeast mating ; Cell-cell recognition ; Sexual agglutination ; Agglutinins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sex-specific agglutinins from the cell surface of haploid cells of Saccharomyces cerevisiae (X2180, mta and mtα) were purified and analysed. The constitutive agglutinin from mta cells was extractable with 3 mM dithiothreitol. It was shown to be a glycoprotein (3% mannose) with an apparent Mr of 43,000 based on gel filtration, but in SDS-PAGE it behaved as a much smaller molecule (Mr between 18,000 and 26,000). About one in three amino acids was a hydroxyamino acid. Its biological activity was resistant to boiling for 1 h, but sensitive to pronase. Intact mtα cells retained their agglutinability in the presence of dithiothreitol but limited trypsinizing released a biologically active agglutinin fragment. It had an apparent Mr of 320,000 (gel filtration). When analysed by SDS-PAGE, a single diffuse band with an apparent Mr of 225,000 was observed. The protein was 94% (w/w) mannose with a trace of N-acetyl glucosamine. Its biological activity was almost completely lost after boiling for 1 h. Both agglutinins behaved as monovalent molecules and specifically inhibited the biological activity of both noninduced and pheromone-induced cells. Pheromone treatment of mta cells resulted in an apparent 32-fold increase in agglutinin activity at the cell surface, whereas pheromone treatment of mtα cells only doubled the apparent agglutinin activity.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 59 (1983), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Iron-deficient Phaseolus vulgaris L. cv. Prelude developed a high reducing capacity for extracellular Fe(III) at the root surface. This reduction was competitively inhibited by Nitro-Blue Tetrazolium salt (Nitro-BT) which was deposited as a blue precipitate within the epidermis cells of the youngest root parts. Root respiration was not influenced by Nitro-BT. The intracellular reduction of Nitro-BT could largely be prevented by excess extracellular Fe(III)EDTA. Iron-sufficient control plants reduced both extracellular Fe(III)EDTA and intracellular Nitro-BT at a much slower rate. A role of cytosolic NADH or NADPH as direct electron donors for the enhanced Fe(III) reduction at the plasmalemma is indicated. NAD+-3-phosphate dehydrogenase activity was higher in preparations from iron-deficient root parts than in preparations from control root parts. Ferricyanide, dichlorophenolindophenol and phenazine methosulfate were also reduced at an increased rate by iron-deficient roots. We conclude that a trans-plasma membrane electron transfer, mediated by a membrane-bound reductase, is responsible for the reduction of extracellular Fe(III).
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Phytopathology 32 (1994), S. 235-259 
    ISSN: 0066-4286
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Biology
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...