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  • 1
    Electronic Resource
    Electronic Resource
    Ouabain-insensitive active sodium transport in rat jejunum: Evidence from ATPase activities, Na uptake by basolateral membrane vesicles and in vitro transintestinal transport (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 6 (1988), S. 155-164 
    Details
    ISSN: 0263-6484
    Keywords: Jejunum ; ATPase activities ; sodium transport ; basolateral membrane vesicles ; everted intestine ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The basolateral membrane of the jejunal enterocyte of the rat was separated by self-orienting Percoll-gradient centrifugation and further purified from brush border contamination. Pellets were analysed for Mg-, Na- and (Na, K)-ATPase activities. The uptake of 0·02 M NaCl was also followed by the rapid micro-filtration technique. Transintestinal transport of fluid and electrolytes, and cell water, Na and K were determined in the in vitro everted and incubated jejunum.There is ouabain-insensitive Na-ATPase in addition to the well-known (Na, K)-ATPase in the basolateral membrane. These are differently inhibited by furosemide and ethacrynate. Na uptake by osmotically active basolateral membrane vesicles is enhanced by ATP and a further enhancement is obtained if there is intravesicular K. The ATP effect is inhibited differently by strophanthidin, furosemide and ethacrynate. In the everted sac preparation, transintestinal transport of Na and fluid still occurs when the Na/K pump is totally inhibited by ouabain.These experimental results suggest that there is also a ouabain-insensitive Na pump, different from the Na/K pump, in the basolateral membrane.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290060303
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  • 2
    Electronic Resource
    Electronic Resource
    1H-nmr studies of synthetic polypeptide models of Plasmodium falciparum circumsporozoite protein tandemly repeated sequence (1989)
    New York : Wiley-Blackwell
    Biopolymers 28 (1989), S. 225-246 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The major immunodominant region of the coating protein of Plasmodium falciparum sporozoites contains multiple tandem copies of the sequence Asn-Ala-Asn-Pro (NANP). Current efforts for the development of an antisporozoite vaccine are focused on the synthesis of polypeptides reproducing part of the circumsporozoite protein repeat sequence and, in an attempt to relate conformational properties and biological response, 1H-nmr one- and two-dimensional studies of the synthetic models (NANP)2NA and (NANP)6 were carried out in water and water/methanol mixtures, at 400 and 500 MHz. In water, (NANP)6 undergoes fast conformational averaging. At variance, in water/methanol, the molecule appears to adopt an extensive structure, but detailed analysis is impaired by high spectral degeneracy. Based on the results obtained with (NANP)2NA and from preliminary expermints in water/trifluoroethanol, an interpretation is suggested for the (NANP)6 data in water/methanol in terms of a mixed sequence of βI-turns and half-turns (or/and γI-turns) around the positions Ni-1-Pi-Ni+1.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360280124
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  • 3
    Electronic Resource
    Electronic Resource
    Lysine as helix C-capping residue in a synthetic peptide (1997)
    New York : Wiley-Blackwell
    Biopolymers 41 (1997), S. 27-35 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The structure of the synthetic peptide CH3CO (Leu-Ser-Leu-Leu-Leu-Ser-Leu)3Lys-NH2 in trifluoroethanol/water 60/40 (volume ratio) was characterized by two-dimensional nmr spectroscopy. The peptide, closely related to the amphiphilic helix models designed by W. F. DeGrado and co-workers to mimic protein ion channels [(1988) Science, Vol. 240, p. 1177-1181], folds into a regular helix spanning residues 1-20. Evidence for a helix C-terminal capping conformation, involving the terminal lysine residue, was observed from Overhauser effects and checked for consistency by restrained molecular dynamics simulations. The side-chain amino group of Lys22 forms a hydrogen bond with the carbonyl of Leu18, and the distorted helical geometry of the terminal dipeptide allows the inclusion of a water bridge between the backbone NH of the Lys22 residue and the carbonyls of Leu19 and Ser20. © 1997 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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