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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 183 (1959), S. 1828-1828 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The protoplasts were prepared by Lederberg's penicillin method1. Before each experiment the protoplasts were washed free of saccharose with physiological saline. Both protoplasts and vegetative forms of E. coli were used for phagocytic tests made with horse leucocytes. The phagocytic reactions ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 295-302 
    ISSN: 1075-2617
    Keywords: Lactoferrin ; peptide immunosuppressors ; thymopentin analogues ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: It has been found that the disulphide-bridged 231-245 pentadecapeptide loop of the lactoferrin (LF) N-lobe contains a region of immunosuppressive activity. The activity resides within a thymopentin-like sequence (Arg-Lys-Pro-Val-Asp) of the loop. Peptides related to the 575-589 loop of the LF C-lobe differ in their immunomodulatory activity from those related to the 231-245 loop. We ascribe this difference to the replacement of the Asp residue in the 231-245 loop by Thr in the 575-589 loop. Two other fragments of LF which were studied, 27-34 and 309-315, do not manifest any activy in the DTH test (cellular immune response), but, on testing in vivo, stimulate the humoral immune response. The 27-34 fragment is related to the bactericidal and immunostimulative region of LF identified by Bellamy et al. [1]. Our results show that the LF molecule contains, not only the known immunostimulating mini-domain, but also a region endowed with immunosuppressive activity.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 318-324 
    ISSN: 1075-2617
    Keywords: p53 protein ; peptide immunomodulators ; TP5 analogues ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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