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Fibrinogen fibrin from

His other major contribution lies in the mechanism of the formation of fibrin from fibrinogen. He was quick to appreciate the power of the... [Pg.387]

Proteans are insoluble products formed by the action of water, dilute acids and enzymes. These are particularly formed from globulins but are insoluble in dilute salt solutions. Example - myosan from myosin, fibrin from fibrinogen. [Pg.151]

The excess vessel wall fibrin accumulation and atherosclerosis seen as a long-term complication of diabetes may well result from the glycosylation-induced inhibition in fibrinogen (fibrin)-plasmin degradative function and heparin-catalyzed antithrombin III activity. [Pg.38]

Essentially all the experiments on the fibrinogen-fibrin conversion to be discussed here were carried out with the less pure preparations of Seegers and Alkjaersig (1956) before the introduction of the Rasmussen (1955) procedure for the purification of thrombin. It is hoped that the traces of impurities thereby introduced do not vitiate any of the conclusions derived from these experiments. Further discussion of the earlier work on thrombin will be found in the reviews of Seegers (1955) and Scheraga and Laskowski (1957). [Pg.132]

Fig. 73. N-Terminal amino acids in fibrinogen and fibrin from different species. The number of chains correspond to a molecular weight of 350,000 except for horse fibrinogen, where the molecular weight is 600,000. The circles indicate chains with no detectable N-terminal groups (Blomback and Yamashina, 1958). Fig. 73. N-Terminal amino acids in fibrinogen and fibrin from different species. The number of chains correspond to a molecular weight of 350,000 except for horse fibrinogen, where the molecular weight is 600,000. The circles indicate chains with no detectable N-terminal groups (Blomback and Yamashina, 1958).
As indicated in Chapter III, step 1 of the fibrinogen-fibrin conversion is an example of a limited proteolytic reaction in which hydrolysis does not go to completion. Side-chain hydrogen bonding may stabilize the peptide bond in the manner indicated in Chapter III. We shall therefore discuss the reversibility of step 1 and the thermodynamic parameters for the equilibrium (Laskowski et al., 1960b). As in the case of the kinetic experiments discussed in Section 5b, the medium used was 1 molar NaBr at pH 5.3 to prevent polymerization of fibrin monomer, and the analysis for f was carried out using TAMe as a thrombin inhibitor, as already mentioned The equilibrium position was approached from both directions. [Pg.145]

Spraggon, G., et al. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 389 455-462, 1997. [Pg.298]

Prior to May of 1998 when the commercial product was approved by the FDA in the United States, surgeons in this country formed fibrin sealant by using topical bovine thrombin, which is a commercially available product, together with concentrated fibrinogen most frequently obtained from the blood bank. Standard blood bank cryoprecipitate is a good source of concentrated fibrinogen. Also... [Pg.1115]


See other pages where Fibrinogen fibrin from is mentioned: [Pg.179]    [Pg.642]    [Pg.144]    [Pg.179]    [Pg.1611]    [Pg.61]    [Pg.231]    [Pg.138]    [Pg.344]    [Pg.345]    [Pg.47]    [Pg.180]    [Pg.188]    [Pg.871]    [Pg.265]    [Pg.642]    [Pg.393]    [Pg.538]    [Pg.224]    [Pg.642]    [Pg.454]    [Pg.100]    [Pg.290]    [Pg.13]    [Pg.354]    [Pg.364]    [Pg.129]    [Pg.139]    [Pg.210]    [Pg.490]    [Pg.60]    [Pg.165]    [Pg.428]    [Pg.397]    [Pg.533]    [Pg.174]    [Pg.180]    [Pg.144]    [Pg.310]    [Pg.1113]    [Pg.1115]    [Pg.1115]    [Pg.1116]   
See also in sourсe #XX -- [ Pg.30 , Pg.834 ]

See also in sourсe #XX -- [ Pg.834 ]




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