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  • 1
    Electronic Resource
    Electronic Resource
    Chain Structure of Cobra Venom Factor from Naja naja and Naja haje venom (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 15 (1982), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The chain structure of cobra venom factor, whether isolated from Naja naja venom (CVFn) or from Naja haje venom (CVFh), is similar. Both homologous proteins are composed of three disulphide-linked chains (A, B, and C) with apparent molecular weights of 72,000, 54,000, and 27,000–35,000 for CVFn and 68,000, 51,000, and 30,000–32,000 for CVFh. That all three polypeptides are integral parts of CVF was demonstrated by investigation of the chain pattern after partial reduction. Reduction with 1–2 mM dithiothreitol under nondenaturing conditions yielded free B-chain, together with an intermediate product composed of disulphide-linked A- and C-chains. The C-chain was heterogenous when investigated by electrophoresis in polyacrylamide slab gels in the presence of SDS. Similarly, isoelectric focusing of CVFn and CVFh showed a multiplicity of bands in the pH range 5.2–6.4. Limited tryptic digestion resulted primarily in the fragmentation of the B-chain. CVFh is much more sensitive to tryptic attack than CVFn. In all our preparations of CVFh a partial, trypsin-like fragmentation of the B-chain was detectable to various extents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb00659.x
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  • 2
    Electronic Resource
    Electronic Resource
    Generation of Anaphylatoxin Activity Related to C3a, by Treatment of Human Serum with the Nitrogen Nucleophile N2H4 or the Chaotrope KSCN (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 22 (1985), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The present study is concerned with the proteolytic processing of complement component C3 in normal human serum treated with N2M4 or KSCN in the presence of EDTA. Upon incubation with these agents. C3 is first converted to the thiolester-cleaved form (C3i) and thereafter fragmented by factor I. In consecutive, relatively slow steps, spasmogenic and platelet-aggregating activity is released. The active principle shows characteristics of C3a. First, the pretreated sera deactivate guinea pig ileum and platelets towards the action of C3ahog, but not C5a-desArghog. Second, the activity is only stable under conditions causing inhibition of serum carboxypeptidase N. such as in the presence of EDTA or of MERGETPA (DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid). Third, the molecular weight deter mined by gel filtration is in agreement with that of C3a. The release of C3a activity requires conversion of C3 to C3i, as well as the complement-independent generation of proteolytic activity in the pretreated sera. The enzyme releasing C3a activity is a serine esterase probably identical with Hageman factor, kallikrein, or another protease related to the contact system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1985.tb01926.x
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  • 3
    Electronic Resource
    Electronic Resource
    Treatment of Human Complement Components C4 and C3 with Amines or Chaotropic Ions (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 13 (1981), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Treatment of human components C4 and C3 with amines like hydrazine, ammonium hydroxide, and neutral ammonium salts or with chaotropic salts like KSCN und NaBr leads to complete loss of haemolytic activity. The pretreated components are however, still active in formation of soluble C3 convertases. This activity pattern is reminiscent of the activities of C4 and C3 that have been activated by cleavage in the fluid phase. Indeed, the antigenic properties of pretreated C4 and C3 are similar to soluble C4b and C3b. The polypeptide chain structure of pretreated C4 and C3, is, however, identical to that of the untreated components when investigated by SDS gel electrophoresis. Pretreatment even reduces greatly the susceptibility of C4 to cleavage by C1 and of C3 to cleavage by classical and alternative pathway C3 convertases. Pretreated components have lost the ability to combine with EAC1 and EAC142, respectively; this fact explains their failure to exhibit haemolytic activity. In serum, pretreated C4 and C3 are cleaved in a manner similar to C4b and C3b. Amines and chaotropic ions cause the same functional and structural alterations, which are best explained by assumption or a conformational change. A similar transformation can also occur in C4 and C3 during preparation or storage
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1981.tb00152.x
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and Properties of a Complement Inhibitor from Naja haje Venom, Distinct from Known Anticomplementary Factors in Cobra Venom (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 14 (1981), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A complement inhibitor (CI) has been isolated from cobra (Naja haje) venom which is distinct from the two known anticomplementary factors in cobra venom [1], in functional properties as well as structure. CI is a small (mol. wt 26,000, determined by sodium dodecyl sulphate gel electrophoresis), heat-labile glycoprotein; the amino acid composition is that of a globular protein. CI interferes at various steps of the complement sequence, including reactions of the classical and the alternative pathway. No effect was observed on C4 fixation and on the assembly of the membrane attack complex from C6–9 (minor inhibiting effects, if present, have not been excluded). Initiation of the alternative pathway is inhibited by CI already at the stage of cleavage of factor B. CI binds to C4, C4b. C3 and C3b: since the major inhibitory action of CI is lost after washing of cell intermediates, complex formation and, as a consequence, steric hindrance may be responsible for the inhibiting effects of CI. CI also interferes with binding of C3b to C3b receptors on human erythrocytes. CI is non-toxic in mice when given intraperitoneally in doses of 5 μg/g.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1981.tb00190.x
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  • 5
    Electronic Resource
    Electronic Resource
    Incompatibility between Complement Components C3 and C5 of Guinea-Pig and Man, an Indication of their Interaction in C5 Activation by Classical and Alternative C5 Convertases (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 9 (1979), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The use of heterologous combinations of guinea-pig and human complement components for titration of C5 with Convertases of the alternative and classical pathway has been investigated. In addition to the known unfavourable combination of C2hu with C4gp partial incompatibilities were detected between heterologous C3 and C5 as well as between C2hu and C5gp. The incompatibility between heterologous C3 and C5 is of special interest since it indicates an interaction of these two non-enzymic components. Concomitant binding studies have demonstrated that a reduced efficiency of C5 Convertases correlates with decreased binding affinity of surface-fixed C3b for C5 when heterologous components are offered. Hence, the present studies give further evidence that surface-bound C3b has the function of a co-factor which binds C5; this interaction is required for C5 activation via the classical as well as the alternative pathway, i.e. by the C3/C5 Convertases 〈inlineGraphic alt="inline image" href="urn:x-wiley:03009475:SJI69:SJI_69_mu1" location="equation/SJI_69_mu1.gif"/〉 and 〈inlineGraphic alt="inline image" href="urn:x-wiley:03009475:SJI69:SJI_69_mu2" location="equation/SJI_69_mu2.gif"/〉.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1979.tb02708.x
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  • 6
    Electronic Resource
    Electronic Resource
    Function of the activated fourth component of complement (C4b) in activation of C2
    Amsterdam : Elsevier
    FEBS Letters 144 (1982), S. 195-198 
    Details
    ISSN: 0014-5793
    Keywords: C1 ; C2 ; C3 convertase formation ; C4 ; Cobra venom ; Complement activation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(82)80636-4
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  • 7
    Electronic Resource
    Electronic Resource
    Function of the activated fourth component of complement (C4b) in activation of C2 (1982) FEBS Letters 144, 195-198.
    Amsterdam : Elsevier
    FEBS Letters 148 (1982), S. 169 
    Details
    ISSN: 0014-5793
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(82)81283-0
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