PubMed · 6910160
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
M J Pineau. 1980-11-05. [Calciparin].. https://pubmed.ncbi.nlm.nih.gov/6910160/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Many surgical patients receive either unfractionated or low-molecular weight heparin in a prophylactic or therapeutic intention. Feared upon the administration of heparin is the heparin-induced thrombopenia (HIT). In HIT type 1, the heparin directly interacts with the platelets. The platelet count rarely falls below 100,000/microliter and normalizes again despite continuous administration of heparin. In HIT type 2 or HIT with thrombosis (HITT) the platelet count usually falls more than 50% and due to an antibody-dependent platelet activation, thromboembolic episodes may occur. Compared to non-surgical patients, the incidence of HITT in the postoperative phase is markedly increased. In suspicion of a HITT, heparins should immediately be stopped and replaced by an alternative coagulant because of a high risk of further thromboembolic complications. Direct thrombin-inhibitors such as the recombinant hirudins are considered to be safe and effective. They have no heparin-like immunological properties and therefore, they seem to become the therapeutic and prophylactic "gold-standard" in patients with HITT.
Theoretical aspects of the thermodynamic characterization of cooperative protein interactions with non-specific segments of a linear polymer lattice have been re-examined. This reconsideration has not only provided an alternative derivation of recursive expressions for the stoichiometry of random ligand binding prior to elimination of the parking problem but also extended that treatment to include binding with overlap of additional lattice units. The major obstacle to thermodynamic characterization of non-specific protein-polymer interactions is determination of the lattice capacity for ligand, which in turn defines the length of the polymer segment to which the protein binds. Although these parameters are most readily obtained from studies under conditions that ensure essentially stoichiometric interaction, the endpoint of such a titration is likely to reflect the irreversible rather than the equilibrium binding capacity of the lattice for ligand. Consideration of published results for spectrofluorometric titrations of the thrombin-heparin system under stoichiometric conditions in such terms has permitted their reconciliation with results of a later publication on the interaction under equilibrium conditions.
Explore the source record for details and available documents.