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  • 1
    Electronic Resource
    Electronic Resource
    Evidence for the transit of aminopeptidase N through the basolateral membrane before it reaches the brush border of enterocytes (1987)
    Springer
    The journal of membrane biology 96 (1987), S. 19-25 
    Details
    ISSN: 1432-1424
    Keywords: aminopeptidase ; brush border ; cell polarity ; intracellular transport ; membrane biogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary In vivo pulse-chase labeling of rabbit jejunum loops was used in conjunction with subcellular fractionation and quantitative immunoprecipitation to determine whether or not the newly synthesized aminopeptidase N transits through the basolateral membrane before it reaches the apical brush border, its final localization. The kinetics of the arrival of the newly synthesized enzyme in the Golgi complex, basolateral and brush border membrane fractions strongly suggest that on leaving the Golgi aminopeptidase N is transiently integrated into the basolateral domain before reaching the brush border.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869331
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Subcellular fractionation and subcellular localization of aminopeptidase N in the rabbit enterocytes (1986)
    Springer
    The journal of membrane biology 89 (1986), S. 53-63 
    Details
    ISSN: 1432-1424
    Keywords: aminopeptidase N ; enterocyte ; cell polarity ; fluorometry ; biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A fast and easy procedure is proposed for preparing concomitantly from the same sample of intestinal mucosa of A+ rabbits, four fractions high enriched in the brush-border and basolateral plasma membrane domains, rough endoplasmic reticulum, and smooth endoplasmic reticulum plus Golgi apparatus membranes, respectively. This is the first time the technique of flow fluorometry has been applied to characterize the brush-border and basolateral membrane fractions using polyclonal or monoclonal antibodies against antigens common to or specific for these two plasma membrane domains. This technique definitely proves the presence of aminopeptidase in at least 60% of the basolateral membrane vesicles, where its level is about 4.5% of that in the brush-border membrane vesicles. The endoglycosidase H-sensitive intermediate of glycosylation of aminopeptidase N in the steady state is accumulated in both the rough and smooth endoplasmic reticulum membranes. Although the rough membrane is more extensive it contains only about 40% of this transient form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870895
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Biosynthesis and intracellular pool of aminopeptidase N in rabbit enterocytes (1985)
    Springer
    The journal of membrane biology 83 (1985), S. 139-146 
    Details
    ISSN: 1432-1424
    Keywords: intestine ; aminopeptidase N ; biosynthesis ; glycoproteins ; A antigenicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A papain treatment at 15°C and pH 7.3 of a microsomal fraction from rabbit enterocytes quantitatively releases the aminopeptidase N integrated in the plasma membranes without solubilizing the enzyme integrated in the intracellular membranes. Working on A+ rabbits, characterized by the presence on the brush-border hydrolases of glycans corresponding to the human blood group A-determinant structure, it was possible to separate the intracellular aminopeptidase into two major molecular forms with or without these determinants. The molecular form devoid of human blood group A antigenicity corresponds to the only stable intermediate of glycosylation, bearing N-linked high mannose oligosaccharides. This endoglycosidase H-sensitive form is fully active and represents in the steady state about 1% of the total cellular aminopeptidase. It contains a cytoplasmic sequence of about 3000 daltons that has not yet been detected in the mature form. The A antigenicity is acquired simultaneously with processing of high mannose glycans to complex glycans. Pulse chase labeling of jejunum loops with [35S]-methionine showed that the complete processing of the transient form synthesized during 10 min takes 1 hr. During the last 30 min of processing, all the newly transformed molecules are transported to the plasma membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868745
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    Paper (German National Licenses)
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