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  • 1
    Electronic Resource
    Electronic Resource
    Recombinant and tissue-derived mouse BM-40 bind to several collagen types and have increased affinities after proteolytic activation (1997)
    Springer
    Cellular and molecular life sciences 53 (1997), S. 478-484 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Calcium binding; collagen affinity; extracellular matrix; kinetic analysis; matrix metalloproteinase.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The calcium-binding extracellular matrix protein BM-40 was obtained as a mouse cDNA product from a stably transfected kidney cell clone. Electrophoresis and N-terminal sequence analysis demonstrated absence of the proteolytic processing previously observed for a mouse tumour-derived BM-40. Yet the two forms of BM-40 were very similar in their CD spectra, their calcium-dependent change in α helix content and their immunological epitopes. In surface plasmon resonance assays, recombinant mouse BM-40 showed distinct binding to the triple-helical domains of collagens I, II, III, IV and V with Kd=1–4 μM but no binding to collagen VI. These interactions were abolished in the presence of EDTA. Tissue-derived mouse BM-40, however, bound collagens I and IV with Kd=0.1–0.2 μM. Activation of collagen binding to give a similar Kd could be achieved for recombinant mouse BM-40 by treatment with the matrix metalloproteinase collagenase-3. The major cleavage site was located in helix C of the extracellular calcium-binding module of BM-40 and other less prominent cleavages occurred close to the N-terminus. The sensitive helix C site was just one residue away from that sensitive to endogenous tissue proteolysis, suggesting that cleavage could be a physiological mechanism to modulate collagen binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000180050059
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  • 2
    Electronic Resource
    Electronic Resource
    Zur Totalsynthese von Human-Sekretin (1993)
    Springer
    Monatshefte für Chemie 124 (1993), S. 577-586 
    Details
    ISSN: 1434-4475
    Keywords: Gastrointestinal hormone ; Human-secretin ; Synthetic peptide factors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The synthesis of the heptacosapeptide amide with the primary structure of Human-secretin is described. For this purpose 7 fragments were designed, i.e. H-Gly-Leu-Val-NH2 〈25–27b〉,Z-Arg(Z 2)-Leu-Leu-Gln-OH 〈21–24〉,Z-Arg(Z 2)-Leu-Gln-OH 〈18–20〉,Z-Arg(Z 2)-Glu(OtBu)-Gly-Ala-OH 〈14–17〉,Z-Arg(Z 2)-Leu-OH 〈12–13〉,Z-Thr(tBu)-Ser(tBu)-Glu(OtBu)-Leu-Ser(tBu)-OH 〈7–11〈,Adoc-His(Adoc)-Ser(tBu)-Asp(OtBu)-Gly-Thr(tBu)-Phe-OH 〈1–6〈 these fragments were consequently assembled to the overall protected total sequence using the Wünsch/Weygand-method with dicyclohexylcarbodiimide. After deprotection by exposure to trifluoroacetic acid in presence of 1,2-ethanedithiol and water as scavenger, the isolated crude product was purified by column chromatography on CM-Sepharose, fast flow. This synthetized Human-secretin showed the full biological activity in comparison to Porcine-secretin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00819525
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  • 3
    Electronic Resource
    Electronic Resource
    New synthesis of somatostatin according to the S-tert-butylthiocysteine procedureSome of the results of this paper were presented in a preliminary communication at the Second FRG-USSR Symposium on Chemistry of Peptides and Proteins, Grainau-Eibsee/Bavaria, May 24-27, 1978: Moroder, L., Musiol, J., Scharf, R., and Wünsch, E. (1978) in Proceedings, pp. 24-25. (1981)
    New York : Wiley-Blackwell
    Biopolymers 20 (1981), S. 17-37 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: To exemplify the usefulness of the S-tert-butylthio group for a reversible blocking of the cysteine thiol function in peptide synthesis, fully protected dihydrosomatostatin was prepared by the fragment-condensation procedure. The experimental results confirm the excellent stability of the asymmetric disulfide under the normal conditions of peptide synthesis and prove that the selective, acid-catalyzed nucleophil removal - as well as by mercaptans - of the 2-nitrophenylsulfenyl group proceeds smoothly in the presence of this thiol protection. Thus, the strategy of overall acid-labile side-chain protection in combination with the Nα-2-nitrophenylsulfenyl group for the chain-elongation steps can be successfully applied to the synthesis of cysteine-containing peptides using their S-tert-butylthio derivatives. Removal of the acid-labile groups, followed by reductive cleavage of the asymmetric disulfides and successive air oxidation, allowed a clean conversion of protected dihydrosomatostatin into somatostatin at a high degree of purity and in good yields.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1981.360200103
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