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Biomedical subjects

M J Gallimore

Publications and source records attributed to M J Gallimore.

At least 73 records · Page 4Linked to original sources
PubMed1979

Changes in antiplasmin and plasmin activities during extreme hemodilution and open heart surgery in dogs.

The effects of extreme hemodilution and open heart surgery on antiplasmin and plasmin activities were investigated in dogs. Assays for plasmin and antiplasmin activities were performed with a chromogenic peptide substrate for plasmin. After hemodilution and during cardiopulmonary bypass (CPB), plasmin activity on the substrate was observed and levels of both "fast-reacting" and "total" antiplasmins fell. The plasmin activity was shown to be due to the formation of alpha2-macroglobulin-plasmin complex which exhibited amidolytic activity on the chromogenic substrate. The falls in antiplasmin activity together with the appearance of the alpha2-macroglobulin-plasmin complex revealed that activation of the fibrinolytic system had occurred. After the operation and following reinfusion of autologous blood, decreased plasmin and increased antiplasmin activities were observed. On the first and sixth days following the operation plasmin activities were still slightly higher than pre-operation values, whilst antiplasmin activities were normal.

Animals↗
PubMed1978

Changes in plasma levels of prekallikrein, kallikrein, high molecular weight kininogen and kallikrein inhibitors during lethal endotoxin shock in dogs.

Plasma levels of prekallikrein, kallikrein, high molecular weight kininogen and kallikrein inhibitors were measured in samples from dogs infused with E. coli endotoxin. Markedly reduced levels of prekallikrein and high molecular weight kininogen were seen at circulatory collapse and free kallikrein was detected. Both 'fast-reacting' and 'time-dependent' inhibitors of plasma kallikrein were significantly reduced. Fractionation of pre-infusion and collapse samples by gel filtration together with immunological procedures indicated that both alpha2-macroglobin and alpha1-antitrypsin were the major kallikrein inhibitors in dog plasma, and that they were significantly reduced in the collapse samples.

Animals↗
PubMed1978

Alterations of plasmin activity, plasminogen levels and activity of antiplasmins during endotoxin shock in dogs.

Spontaneous plasmin activity and 'fast-reacting' and 'time-dependent' antiplasmin activities were determined during various stages of canine endotoxin shock by means of assays utilizing a chromogenic tripeptide derivative (S-2251, Kabi AB, Peptide Research Division, Mölndal). During shock, gradually decreasing values of both antiplasmins were found, revealing most pronounced falls of 'fast-reactin' antiplasmin. These changes of plasma antiplasmin activities were accompanied by decreasing values of plasminogen and evidence of plasmin activity. Immunochemical determination of plasma levels of alpha2-macroglobulin (alpha2-M) and alpha1-antitrypsin (alpha1-AT) and gel filtration studies, demonstrated marked falls in levels of alpha2-M and alpha2-plasmin inhibitor and small reductions of alpha1-AT in this state.

Animals↗
PubMed1975

Serum inhibitors in fibrinolysis.

Four protease inhibitors have been identified in human serum and methods for their isolation are described. After removal of the euglobulin fraction, serum was submitted to ion exchange chromatography and gel filtration, and fractions were tested for inhibition of the lysis of plasminogen-deficient fibrin clots by plasmin, trypsin and elastase. In addition inhibitors of plasminogen activation were sought by studying the effects of separated fractions on the lysis of plasminogen-rich fibrin clots by urokinase. Examination by immunophoresis showed that three of the separated inhibitors were alpha2-macroglobulin, alpha1-antitrypsin and inter-alpha-trypsin inhibitor. The fourth antiprotease was a powerful inhibitor of both urokinase-induced and plasmin-induced clot lysis, and was identified as an inter-alpha-globulin from its electrophoretic mobility in agarose gels.

Chemical Fractionation↗
PubMed1972

The origin of fibrin breakdown products and the interpretation of their appearance in the circulation.

It has been shown that the incubation of human plasma with urokinase at a concentration sufficient to cause rapid lysis of the clots formed on the addition of thrombin does not give rise to the production of measurable concentrations of non-clottable fibrinogen breakdown products. Also, breakdown products could not be detected in the course of experiments in vivo when urokinase was administered to monkeys and only in very low concentrations when a fibrinolytic state was induced by exercise in three healthy human volunteers. In contrast, high concentrations of breakdown products were found after thrombin infusion into monkeys. It is concluded that circulating fibrinogen is not readily broken down into non-clottable products by the fibrinolytic enzymes, and that normal animals and healthy human subjects do not have substantial deposits of fibrin that are available for breakdown during a fibrinolytic episode. The presence of breakdown products in the circulation is therefore likely to be indicative of the fibrinolytic response to an initial coagulation event.

Adult↗
PubMed1967

Effect of diluents on blood clot lysis.

One of the current methods used for measuring natural fibrinolytic activity in blood involves dilution of the blood with phosphate buffer. An adaptation of this method using a solution of sodium acetate as diluent is described. Evidence is given to show that dilute blood clots lyse not only because of the dissociation of an antiplasmin-plasmin complex, but also by virtue of a reduction of the intrinsic chloride ion concentration.

Acetates↗
PubMed1965

A comparative study of the inhibitors of fibrinolysis in human, dog and rabbit blood.

Comparison of sera from dog, rabbit and man shows that dog serum contains most fibrinolytic inhibitor and human serum least. The inhibitors are potentiated by a variety of inorganic salts, of which sodium chloride is most effective. Euglobulin fractions precipitated from rabbit and human plasma at pH 5.3 contain small amounts of inhibitory material, whereas little remains in the corresponding dog euglobulin or in euglobulins from all three species when precipitated at pH 6.0. The potentiation of fibrinolytic inhibitors by sodium chloride differs between the three species, suggesting that their composition is not identical. Chloroform extraction removes a proportion of the inhibitory material from each serum.

Animals↗