Attempts to isolate C′3 activity from pig serum

Pontieri, G. M.; Cotrufo, M. Francesca; Ciccimarra, F; Tolone, G.

doi:10.1007/bf02144749

Cited by 5 publications

(3 citation statements)

References 3 publications

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“…The finding that SPS precipitated beta lipoproteins and fibrinogen confirmed previous observations (2,17). Two-dimensional immunodiffusion studies disclosed that SPS also precipitated beta 1C-globulin (C3) and C4 from fresh human serum; previously Pontieri et al (10) demonstrated that SPS inactivated C3 in porcine serum. Thus the anticomplementary activity of SPS appears to be due to the precipitation of at least two components of human complement, namely C3 and C4.…”

Section: Discussionsupporting

confidence: 88%

Anticomplementary, Anticoagulatory, and Serum-Protein Precipitating Activity of Sodium Polyanetholsulfonate

Traub¹,

Lowrance²

1970

Applied Microbiology

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ment-mediated hemolysis of 1:10 diluted fresh guinea pig and human serum; at least twice as much SPS was required to reduce complement activity in 1: 2 diluted human serum. The coagulation of 90 and 20% human blood was inhibited by 250 and 125 Ag of SPS per ml, respectively. When added to fresh human serum, SPS precipitated beta iC-globulin (C3), C4, beta lipoproteins, immunoglobulin IgG, IgM, and IgA, though incompletely.

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Section: Discussionsupporting

confidence: 88%

Anticomplementary, Anticoagulatory, and Serum-Protein Precipitating Activity of Sodium Polyanetholsulfonate

Traub¹,

Lowrance²

1970

Applied Microbiology

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“…The precise nature of the inhibitory effect of SPS against the activation of human complement via the classical and alternative pathways remains to be elucidated. It has been demonstrated that SPS interacted with the first (Cl) and third (C3) components of human complement (11,13,18,22). Furthermore, Klein (7) had observed the inactivation of "CM," a heatlabile, ammonium-resistant component of complement.…”

Section: Discussionmentioning

confidence: 99%

Inactivation of classical and alternative pathway-activated bactericidal activity of human serum by sodium polyanetholsulfonate

Traub¹,

Kleber²

1977

J Clin Microbiol

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Sodium polyanetholsulfonate (SPS) at a final concentration of at least 250 microng/ml (0.025%) was required for inhibition of the bactericidal activity of 80% (vol/vol) of fresh human serum against "promptly serum-sensitive" strains of Serratia marcescens and control strain Escherichia coli C, i.e., for inhibition of the classical pathway of complement activation. In contrast, SPS at 125 microng/ml (0.0125%) was sufficient for neutralization of the bactericidal activity of 80% (vol/vol) fresh human serum against "delayed serum-sensitive" strains of S. marcescens known to activate the alternative pathway of human complement. Addition of up to 500 microng of SPS per ml to 80% (vol/vol) fresh human serum failed to neutralize transferrin-mediated, "late" bacteriostasis against control strain E. coli C, an effect that was demonstrable only after prolonged, i.e., overnight, incubation of the test strain. However, this late inhibitory effect against E. coli C was not observed in SPS-treated 20% (vol/vol) fresh human serum or in 10 or 20% (vol/vol) conventionally heat-inactivated human serum. Immunoelectrophoretic examination disclosed that SPS did not precipitate transferrin from either fresh or heat-inactivated human serum. Thus, SPS, at 250 microng/ml, was demonstrated to be sufficient for the inhibition of both classical and alternative complement pathway-activated bactericidal activity of 80% (vol/vol) human serum. However, SPS at a concentration of 500 microng/ml failed to antagonize one antimicrobial system of 80% (vol/vol) human serum, namely transferrin-mediated bacteriostasis.

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“…Interaction between liquoid and other plasma proteins, such as complement com ponents [11][12][13][14] Prolongation of clot lysis in purified sys tems as a result of preincubation of plasmin ogen with liquoid was found with both uro kinase and streptokinase. In similarity with the chromogenic experiments, clot lysis in duced by streptokinase was more susceptible to inhibition by liquoid than when urokinase was used as the activator.…”

Section: Analytical Ultracentrifugationmentioning

confidence: 99%

Inhibition of Fibrinolytic System by Liquoid (Polyanetholesulfonate)

Gilboa¹,

Ryan

MacColl

1987

Pathophysiol Haemos Thromb

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Liquoid induces microvascular thrombosis and renal cortical necrosis in experimental animals. We hypothesized that thrombosis and renal cortical necrosis may, at least in part, result from the inhibition of the fibrinolytic system by liquoid. Effects of liquoid on plasminogen activation by rat kidney, purified human tissue plasminogen activator (TPA), urokinase, streptokinase, and on the amidolytic activities of TPA, urokinase, and plasmin were studied using chromogenic substrates and clot lysis. Liquoid had a strong inhibitory effect on the fibrinolytic system in vivo and in vitro. The inhibition was most effective at the plasminogen activation level, with activation by streptokinase being most susceptible. The demonstrated stoichiometric binding between liquoid and plasminogen, and to a lesser degree the direct inactivation of plasminogen activators and plasmin, is probably responsible for the reduction of plasminogen activation in circulation and in the kidneys.

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Attempts to isolate C′3 activity from pig serum

Cited by 5 publications

References 3 publications

Anticomplementary, Anticoagulatory, and Serum-Protein Precipitating Activity of Sodium Polyanetholsulfonate

Anticomplementary, Anticoagulatory, and Serum-Protein Precipitating Activity of Sodium Polyanetholsulfonate

Inactivation of classical and alternative pathway-activated bactericidal activity of human serum by sodium polyanetholsulfonate

Inhibition of Fibrinolytic System by Liquoid (Polyanetholesulfonate)

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