Bovine Plasmin Research Articles

Effect of streptokinase, epinephrine and plasmin on the paroxysmal nocturnal hemoglobinuria serum hemolytic system.

pH-lysis curves have been constructed from data obtained from incubating the erythrocytes of five cases of paroxysmal nocturnal hemoglobinuria (PNH) with autologous and normal acidified sera. The effect of streptokinase, epinephrine and plasmin (bovine and human) on these pH-lysis curves has been investigated. Streptokinase, human plasmin and epinephrine had little or no effect on these pH-lysis curves when added to the acid serum-PNH red cell suspenson just prior to incubation at 37°C. A period of preliminary incubation was necessary to demonstrate the inhibitory effect of these substances on the PNH serum hemolytic system. This suggests that these reagents react with something in the serum. No inhibition could be demonstrated after preliminary incubation of PNH erythrocytes with streptokinase, plasmin and epinephrine. Small concentrations of bovine plasmin added directly to the acid serum-PNH red cell suspension enhanced the PNH hemolytic activity; high concentrations completely inactivated the PNH hemolytic system. Bovine plasmin by itself in small concentrations was not hemolytic. Thrombin failed to reactivate the PNH hemolytic mechanism of the streptokinase-, and plasmin-treated sera. The addition of thrombin restored completely the hemolytic activity of epinephrine-treated sera. Submitted on June 22, 1959

Healing of infected wounds treated with human plasmin and hyaluronidase; débridement and healing of infected wounds, several with metallic foreign bodies.

Enzyme therapy of infected wounds and ulcerating lesions is a rapidly developing field, in which there is great promise. It is said that John Hunter used crude pancreatic enzymes in the treatment of wounds. The maggot treatment of dirty chronic infected wounds and osteomyelitis cavities was undoubtedly effective because of proteolytic enzymes secreted by the maggots. 1 The modern methods of enzyme treatment using purified materials have been developed only in recent years. 2 Papain 3 was used as long ago as the First World War for cleansing of infected burns and dirty wounds but was abandoned because of the severe irritation it caused. It was with streptokinase and streptodornase 4 that the first well-controlled studies of this type of therapy were made. 5-8 Trypsin, a proteolytic enzyme obtained from the pancreas, is a stronger digestive enzyme, which has been used with success in debridement. 9-11 Bovine plasmin (fibrinolysin) has

In vivo fibrinolytic activity and pharmacology of various plasmin (fibrinolysin) preparations.

A quantitative method based on the disappearance of I 131 labeled fibrin has been used to study the in vivo effect of fibrinolytic agents. Various preparations of human and bovine plasmin were found to lyse clots effectively. The minimal effective dose of human plasmin prepared by the method of Kline was 15 Loomis units/Kg. Plasmin preparations given intravenously produced hypotension and leukopenia followed by leukocytosis. Doses above 30 Loomis units/Kg. caused decrease in fibrinogen level and clotting index.

Formation and properties of the activator of plasminogen and of human and bovine plasmin.

Formation and properties of the activator of plasminogen and of human and bovine plasmin.

Activation of bovine plasminogen by trypsin.

SummaryCrude bovine plasminogen was activated to plasmin by trypsin, by chloroform treatment which allowed an autocatalytic type activation, or by chloroform treatment followed by rapid activation with a low level of trypsin. Since the last method was an efficient one, other proteases were tried in the place of trypsin. Pancreatin and partially purified bovine plasmin also activated crude plasminogen but chymotrypsin, ficin and papain did not. Trypsin was the best activator of the series tested. Partially purified plasmins activated by trypsin, chloroform, or chloroform-trypsin were lyophilized and compared with one another. The plasmins prepared by trypsin activation appeared to be more potent

Effect of carboxylic and amino acids on fibrinolysis produced by plasmin, plasminogen activator and proteases.

Summary1. Fibrinolysis produced by activation of plasminogen in bovine fibrin by plasminogen activator preparations from human blood was increased considerably by di-and tri-carboxylic acids and decreased by diaminomonocarboxylic acids. 2. Fibrinolytic activity of a number of proteases was generally not significantly influenced. Bovine plasmin was moderately inhibited by lysine.

The influence of calcium ions on the inactivation of human complement and its components by plasmin.

Ca(++) potentiates the inactivation of human complement by streptokinase-activated plasmin and chloroform-activated bovine plasmin. The optimum concentration of Ca(++) varies between 10(-2)M and 10(-3)M, decreasing with increasing concentrations of streptokinase. The susceptibility of the components of complement to inactivation by plasmin is different in the presence and absence of Ca(++). C'2 and C'4 are most readily inactivated by plasmin in the presence of Ca(++), while C'1 disappears first in the absence of Ca(++). A large part of this C'1 disappearance is due to spontaneous inactivation. Similarities are pointed out between the influence of Ca(++) on the inactivation of the components of complement by antigen-antibody systems and by plasmin.

The inactivation of complement and its components by plasmin.

Human complement is inactivated by plasmin, the proteolytic enzyme of plasma or serum active at or near neutrality. The addition of streptokinase to human serum, which converts plasminogen to plasmin, also causes the inactivation of complement components C'2 and C'4 and varying amounts of C'1. C'3 is the most resistant to inactivation by plasmin. Chloroform-activated human plasmin and bovine plasmin also destroy these components of complement, but are less effective than the streptokinase-activated enzyme. The inactivation of complement by the addition of streptokinase to human serum is inhibited by high hydrogen ion concentrations, low temperature, and elevated ionic strength. The inactivation of the components of complement in various fractions of serum is influenced by the available plasminogen and the content of plasmin inhibitors in these fractions. Certain similarities are pointed out between the components of complement and the factors in the plasmin system and between the inactivation of the components of complement by antigen-antibody reactions, by specific agents, and by plasmin. The possible significance of these relationships in immune hemolysis and complement fixation, and the possible role of the plasmin system in the instability of complement and the development of anticomplementary properties in serum are discussed.

Activation of Plasminogen by Trypsin and Plasmin

Abstract Incubation of human or bovine plasminogen with trypsin or bovine plasmin resulted in the production of increased fibrinolytic activity, indicating that plasminogen is converted into plasmin under these conditions. Chymotrypsin under idential conditions was found not to possess this property.

Fibrinokinase.

Summary.1. For the preparation of fibrinokinase of high activating power, fresh pig hearts are needed. The mode of preparation appears to be of minor importance.2. The extent of inactivation of bovine plasmin by fibrinokinase is not directly related to the activating power of the fibrinokinase sample. It appears that a decreased activating power may be caused either by a simple destruction of the activating substance or by its combination with a blocking substance. Only in the last case is a high inactivating power towards plasmin developed.3. Different means were tried without success for accelerating the activation process.4. The low activating power of fibrinokinase towards human plasminogen has been confirmed. On the other hand, streptokinase‐activated human plasmin is inactivated by samples of fibrinokinase apparently in the same manner as is bovine plasmin.