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  • 1
    Electronic Resource
    Electronic Resource
    Effects of tumor necrosis factor-α on connective tissue metabolism in normal and scleroderma fibroblast cultures (1993)
    Springer
    Archives of dermatological research 284 (1993), S. 440-444 
    Details
    ISSN: 1432-069X
    Keywords: Tumor necrosis factor-α ; Normal fibroblasts ; Scleroderma fibroblasts ; Connective tissue metabolism ; Gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Recent studies have demonstrated that tumor necrosis factor-α(TNF-α) selectively decreases production of collagens I and III, the major types of collagen in the dermis, and increases production of collagenase in cultured dermal fibroblasts. The effects of TNF-α on collagens I, III and VI, fibronectin and collagenase gene expression by fibroblasts derived from normal individuals and patients with systemic sclerosis (SSc) were studied. SSc is characterized by excessive accumulation of collagen in the skin and in certain organs. TNF-α inhibited collagen production and mRNA levels of collagens I and III and of fibronectin, and stimulated collagenase activity and collagenase mRNA levels in SSs fibroblasts. Levels of mRNA for α1(VI) and α3(VI) collagen and for Β-actin were unaltered in SSc fibroblasts incubated with TNF-α. Similar results were observed for mRNA levels in normal fibroblasts incubated with TNF-α. These results suggest that TNF-α could be expected to be beneficial in the treatment of SSc. In addition, our results indicated that collagen-VI expression is regulated independently from expression of collagens I and III, and expression of fibronectin and collagens I and III are regulated in parallel in fibroblasts treated with TNF-α.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00373353
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  • 2
    Electronic Resource
    Electronic Resource
    Secondary structural changes of chymotrypsinogen A, alpha-chymotrypsin, and the isolated polypeptides Cys1-Leu13, Ile16-Tyr146, and Ala149-Asn245 in sodium dodecyl sulfate, urea and guanidine hydrochloride (1990)
    Springer
    Colloid & polymer science 268 (1990), S. 612-617 
    Details
    ISSN: 1435-1536
    Keywords: Chymotrypsinogen ; chymotrypsin fragments ; CD ; secondary structure ; sodiumdodecylsulfate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Secondary structural changes of chymotrypsinogen A,α-chymotrypsin, and their isolated polypeptides Cys1-Leu13, Ile16-Tyr146, and Ala149-Asn245were examined in aqueous solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride (residue numbers from chymotrypsinogen). After the fragmentation by the cleavage of disulfide bridges inα-chymotrypsin, the helical structure was formed in the isolated polypeptide 16–146 where the helical segments do not exist in the protein state. The polypeptide 149–245, where the helical segments of the parent protein are originally located, contained no helices. The polypeptide 1–13 was almost disordered. The three polypeptides, chymotrypsinogen,α-chymotrypsin and the polypeptide 16–146, clearly showed differences in the stabilities of helical structures in solutions of urea and guanidine hydrochloride. The addition of SDS accelerated the formation of helical structures in each polypeptide except for 1–13.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01410401
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Kinetic study of ion exchange reaction between lysozyme and carboxymethyl Sephadex C-25 (1992)
    Springer
    Colloid & polymer science 270 (1992), S. 878-884 
    Details
    ISSN: 1435-1536
    Keywords: Adsorption-desorptionkinetics ; kinetics ; ionexchange ; lysozyme ; Sephadex C-25
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract The ion-exchange reaction of lysozyme with carboxymethyl Sephadex C-25 was followed by conductivity change as a function of time just after the rapid mixing of the protein solution with the Sephadex suspension. A single relaxation process was observed; the conductivity increased exponentially with time in the 100 s scale. In this process, protons were released from the Sephadex C-25 in the same time scale. The relaxation process slowed down with an increase in the lysozyme concentration, but it quickened upon the addition of HCl. On the other hand, the ζ potential on the Sephadex C-25 surface changed from a negative value to a positive one with an increase in the amount of lysozyme adsorbed on the surface. On the basis of these data, the relaxation process was attributed to the ion-exchange reaction of lysozyme with several protons of carboxymethyl groups of the Sephadex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00657732
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    Paper (German National Licenses)
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