Evidence of Antithrombic Activity of the Anticoagulant Fraction of Incubated. Fibrinogen

Triantaphyllopoulos, D. C.; Triantaphyllopoulos, E.

doi:10.1111/j.1365-2141.1966.tb05618.x

Cited by 19 publications

(7 citation statements)

References 12 publications

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“…23 25 Various fragments of FDP-fdp are known to interfere with thrombin activation, fibrin polymerization, and platelet function. 26 27 An electron microscopically indentifiable abnormality in clot structure has also been described,28 which apparently is caused by fragments of normal plasma protein that can alter the functional capacity of a fibrin clot and contribute to a hemorrhagic diathesis.…”

Section: Therapy and Prevention-thrombolysismentioning

confidence: 99%

Hemorrhage and the products of fibrinogen digestion after intracoronary administration of streptokinase.

Timmis¹,

Gangadharan²,

Ramos³

et al. 1984

Circulation

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Hemorrhage was prospectively identified in 26 of 116 consecutive patients (23%) who were receiving intracoronary streptokinase for occlusive coronary thrombi producing infarction. Bleeding was not influenced by the dose of streptokinase or the method of cardiac catheterization. Before treatment, prothrombin time and partial thromboplastin time were normal in both bleeders and nonbleeders. Fibrinogen levels measured by bioassay after streptokinase (mean + SEM) were 62 29 mg/dl in patients with major bleeding, 1 11 ±+ 26 mg/dl in patients with minor bleeding, and 109 + 13 mg/dl in nonbleeders (p -NS). The regression slope b calculated from poststreptokinase fibrinogen time-concentration data in 71 patients was 4.7 mg/dl/hr. However, mean fibrinogen concentrations calculated at sequential 5 hr intervals revealed no net regeneration for the first 20 hr after thrombolysis. The apparent fibrinogen regeneration rate was less than normal (31 mg/kg/day) for more than 10 hr but subsequently increased to 94 10 mg/kg/day by the second day. The initial apparent latency of fibrinogen regeneration paralleled the sharp rise in fibrinogen degradation products, which began to decline after 20 hr of treatment but remained elevated well into the second day. Because of their anticoagulant effects, these products may interfere with the fibrinogen assay, causing spuriously low results. Thus, whether the early delay in fibrinogen regeneration is real or simply a reflection of the effects of fibrinogen degradation products on the bioassay, it signals the time for caution in initiating systemic-heparin therapy.

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Section: Therapy and Prevention-thrombolysismentioning

confidence: 99%

Hemorrhage and the products of fibrinogen digestion after intracoronary administration of streptokinase.

Timmis¹,

Gangadharan²,

Ramos³

et al. 1984

Circulation

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“…Our results are also in agreement with the findings of Wallen and Bergstrom (1958), who showed that thrombin uncovers four N-terminal glycine residues in every molecule of plasminolyzed fibrinogen. Finally, Triantaphyllopoulos et al (1966) have isolated the two main electrophoretic fractions of plasminolysed fibrinogen. Since their products were unclottable, they were probably dealing with the D and E fragments.…”

Section: Discussionmentioning

confidence: 99%

Release of Fibrinopep tides from Fibrinolytic Fibrinogen Fragment E

Peyer¹,

Straub²

1973

Thromb Haemost

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Purified “terminal” proteolytic E fragments of fibrinogen and fibrin as produced by plasmin digestion were treated with thrombin. Thrombin treatment of fragment E obtained from fibrinogen, liberated both fibrinopeptides A and B and sometimes AP. Thrombin treatment of fragment E obtained from Reptilase-clotted fibrin liberated only fibrinopeptide B. From fragments E derived from thrombin-clotted fibrin as well as from fragments D obtained from either fibrinogen, thrombin-fibrin or Reptilase - fibrin no fibrinopeptides could be recovered.

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“…Analysis of the results for LPloo showed that only the concentrations of histidine (P <0-01), isoleucine (P = 0.014) and proline (P=0.05) were significantly different from those for fibrinogen. It is pertinent to add here that thrombin cannot split trichloroacetic acid-soluble protein fragments from LP20o and SP20o, but that the evidence indicates that it can split such fragments from LPloo (Triantaphyl-lopoulos & Triantaphyllopoulos, 1966a).…”

Section: Methodsmentioning

confidence: 98%

Amino acid composition of human fibrinogen and anticoagulant derivatives

Triantaphyllopoulos

1967

Biochemical Journal

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1. The amino acid compositions of human fibrinogen and three intermediate anticoagulant derivatives were determined by column chromatography. The derivatives were isolated by ammonium sulphate fractionation and column electrophoresis from solutions of fibrinogen undergoing spontaneous breakdown. One derivative, isolated as the large electrophoretic peak at the end of the clottable period (100% CP) of the parent fibrinogen solution, was labelled LP(100) and others obtained at twice this period (200% CP) were designated as LP(200) and SP(200) (LP, large peak; SP, small peak). 2. Maximal ;molecular' weights of approx. 294000 for LP(100), 137000 for LP(200) and 37000 for SP(200) were calculated for the protein moieties. At least 265 amino acid residues must have been lost from each fibrinogen molecule during the formation of LP(100), and 1362 during the formation of the other two derivatives. 3. Only one derivative (LP(200)) had a partial specific volume ([unk] 0.725ml./g.) different from that of fibrinogen ([unk] 0.721ml./g.). 4. No significant differences in refractive index at 589mmu were detected. 5. Calculation of the total number of ionizable groups/10(5)g. of each protein moiety showed a preponderance of the following numbers of negative charges: 22 in fibrinogen; 24 in LP(100); 26 in LP(200); 49 in SP(200). The isoionic points were estimated to be approx.+0.03pH unit (for fibrinogen), -0.06pH unit for (LP(100)) and +0.28pH unit (for LP(200)) from the pK of imidazole, and 0.78pH unit above the average pK of aspartyl and glutamyl ions (for SP(200)). These figures agree closely with experimentally determined values of the isoelectric point of fibrinogen and its derivatives.

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Evidence of Antithrombic Activity of the Anticoagulant Fraction of Incubated. Fibrinogen

Cited by 19 publications

References 12 publications

Hemorrhage and the products of fibrinogen digestion after intracoronary administration of streptokinase.

Hemorrhage and the products of fibrinogen digestion after intracoronary administration of streptokinase.

Release of Fibrinopep tides from Fibrinolytic Fibrinogen Fragment E

Amino acid composition of human fibrinogen and anticoagulant derivatives

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