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  • LIFE SCIENCES (GENERAL)  (3)
  • Ca++-binding sites  (1)
  • ER endoplasmic reticulum  (1)
  • 2010-2014
  • 1995-1999  (1)
  • 1975-1979  (4)
Collection
Publisher
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  • 2010-2014
  • 1995-1999  (1)
  • 1975-1979  (4)
  • 1980-1984  (11)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 100 (1979), S. 33-43 
    ISSN: 1615-6102
    Keywords: Amoeba proteus ; Ca++-binding sites ; Cytochemical demonstration ; Induced pinocytosis ; Plasma membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Different methods were used to demonstrate the existence of Ca++-binding sites (Ca++-bs) at the plasma membrane ofAmoeba proteus. In pinocytoting animals the number (indicated by the average distanced in nm) and size (average longitudinal axiss in nm) of Ca++-bs at the cytoplasmic surface of the cell membrane were significantly increased (d=162±15;n=41 ands=93±5;n=47) in comparison to controls (d=208 ±21;n=37 ands=59±8;n=45). The ratio of P: Ca obtained by X-ray microanalysis was in the range of 1.5. The differences observed in the two experimental groups of amoebae are explained by conformational changes in the molecular structure and an increased Ca++-permeability of the plasma membrane during induced pinocytosis. Microplasmodia of the acellular slime moldPhysarum polycephalum investigated for comparison were found to have no Ca++-bs at the interior cell surface.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Parasitology research 82 (1996), S. 468-474 
    ISSN: 1432-1955
    Keywords: Abbreviationsaa Amino acids ; BFA brefeldin A ; bp base pairs ; ER endoplasmic reticulum ; FCS fetal calf serum ; HEPES N-(2-5hydroxyethyl)piperazine-N′- (2-ethanesulfonic acid) ; mAb(s) monoclonal antibodies ; NP-40 Nonidet P-40 ; ORF open reading frame ; pSM/1.6 plasmid carrying the cDNA insert ; SDS-PAGE sodium dodecyl sulfate-polyacrylamide gel electro- phoresis ; SRP signal recognition particle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The cDNA clone pSM/1.6 encoding the 26.5-kDa precursor molecule of the 16/17-kDa microneme antigen of Sarcocystis muris cyst merozoites was expressed in a cell-free translation/translocation system to study translocation of the protein across membranes. The antigen was found to be translocated across heterologous endoplasmic reticulum membranes. Translocation was accompanied by cleavage of a signal peptide to create a 23-kDa polypeptide that was completely protected from digestion with proteinase K. Pulse-chase analysis of [35S]-methionine-labeled S. muris cyst merozoites demonstrated that the 16/17-kDa antigen derived from a 23-kDa precursor molecule and that its processing occurred at between a few minutes and 2 h after biosynthesis. This leads to the conclusion that the native microneme antigen is secreted from the parasite cell via the endoplasmic reticulum. Sorting into micronemes might occur during transition through a Golgi-like structure, involving cleavage of the hydrophilic propeptide to create the mature 16/17-kDa protein.
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  • 3
    Publication Date: 2011-08-16
    Description: The activity and stability of the palmitoyl-coenzyme A (CoA) desaturase complex of Saccharomyces cerevisiae was influenced by several factors. Cells, grown nonaerobically and then incubated with glucose, either in air or under N2, showed a marked increase in desaturase activity. Cycloheximide, added during such incubations, prevented the increase in activity, suggesting de novo synthesis. The stability of the desaturase from cells grown nonaerobically was affected by subsequent treatment of the cells; enzyme from freshly harvested cells, or from cells that were then shaken under nitrogen, readily lost activity upon washing or during density gradient analysis, whereas aerated cells, in the presence or absence of glucose, yielded stable enzyme preparations. The loss of activity in nonaerobic preparations could be reversed by adding soluble supernatant from these homogenates and could be prevented by growing the cells in the presence of palmitoleic acid and ergosterol, but not with several other lipids tested.
    Keywords: LIFE SCIENCES (GENERAL)
    Type: Journal of Bacteriology; 124; Nov. 197
    Format: text
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  • 4
    Publication Date: 2011-08-17
    Description: A comparative study of the effects of varying levels of oxygen on some of the metabolic functions of the primitive eukaryote, Saccharomyces cerevisiae, has shown that these cells are responsive to very low levels of oxygen: the level of palmitoyl-Co A desaturase was greatly enhanced by only 0.03 vol % oxygen. Similarly, an acetyl-CoA synthetase associated predominantly with anaerobic growth was stimulated by as little as 0.1% oxygen, while an isoenzyme correlated with aerobic growth was maximally active at much higher oxygen levels (greater than 1%). Closely following this latter pattern were three mitochondrial enzymes that attained maximal activity only under atmospheric levels of oxygen.
    Keywords: LIFE SCIENCES (GENERAL)
    Type: Origins of Life; 9; Sept
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  • 5
    Publication Date: 2011-08-17
    Description: Previous studies on the yeast Saccharomyces cerevisiae have shown that two different forms of the enzyme acetyl coenzyme A synthetase (ACS) are present, depending on the conditions under which the cells are grown. The paper evaluates the usefulness of a method designed to assay both synthetases simultaneously in yeast homogenates. The data presented confirm the possibility of simultaneous detection and estimation of the amount of both ACSs of S. cerevisiae in crude homogenates of this strain, making possible the study of physiological factors involved in the formation of these isoenzymes. One important factor for specifying which of the two enzymes is found in these yeast cells is the presence or absence of oxygen in their environment. Aeration not only affects the ratio of the two ACSs but also appears to affect the cellular distribution of these enzymes. Most of the data presented suggest the possibility that the nonaerobic ACS may serve as a precursor to the aerobic form.
    Keywords: LIFE SCIENCES (GENERAL)
    Type: Journal of Bacteriology; 137; Jan. 197
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