scholarly journals STUDIES ON A PROTEOLYTIC ENZYME IN HUMAN PLASMA. VII. A FATAL HEMORRHAGIC STATE ASSOCIATED WITH EXCESSIVE PLASMA PROTEOLYTIC ACTIVITY IN A PATIENT UNDERGOING SURGERY FOR CARCINOMA OF THE HEAD OF THE PANCREAS 1

1952 ◽  
Vol 31 (5) ◽  
pp. 521-528 ◽  
Author(s):  
Oscar D. Ratnoff
Keyword(s):  
Human Plasma ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Head Of The Pancreas

scholarly journals STUDIES ON A PROTEOLYTIC ENZYME IN HUMAN PLASMA

1950 ◽  
Vol 91 (2) ◽  
pp. 123-133 ◽  
Author(s):  
Oscar D. Ratnoff ◽  
Robert C. Hartmann ◽  
C. Lockard Conley
Keyword(s):  
Human Plasma ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Globulin Fraction ◽  
Considerable Potential ◽  
Normal Platelet

A fraction of globulin was prepared from human plasma which was deficient in prothrombin, thrombin, fibrinogen, plasma thromboplastin, and accelerator globulin. The preparation of globulin contained considerable potential proteolytic activity which could be activated by streptococcal fibrinolysin. This fraction of globulin accelerated the clotting of normal platelet-deficient plasma. However, the clot-accelerating effect of the globulin fraction was the same whether or not its proteolytic property had been activated. The addition of streptococcal fibrinolysin to normal platelet-deficient plasma did not accelerate coagulation. Nor did the addition of streptococcal fibrinolysin to hemophilic platelet-deficient plasma promote its coagulation. The data presented suggest that proteolysis by activated plasma proteolytic enzyme is not an essential stage in the coagulation of the blood.

scholarly journals STUDIES ON A PROTEOLYTIC ENZYME IN HUMAN PLASMA

1948 ◽  
Vol 87 (3) ◽  
pp. 199-209 ◽  
Author(s):  
Oscar D. Ratnoff
Keyword(s):  
Human Plasma ◽  
Proteolytic Enzyme

1. The experiments reported suggest that the plasma proteolytic enzyme activated by streptococcal fibrinolysin is identical with that activated by chloroform. 2. The precursor of this plasma proteolytic enzyme is precipitated with the euglobulin fraction of plasma at pH 5.2.

scholarly journals Lipases Produce Functionally Intact Subunits of Factor VIII (Antihaemophilic Factor)

1977 ◽  
Author(s):  
M. Furlan ◽  
T. Jakab ◽  
E. A. Beck
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Functional Properties ◽  
Functional Activity ◽  
Proteolytic Enzyme ◽  
Gel Filtration ◽  
Phenylmethylsulfonyl Fluoride ◽  
Triglyceride Lipase ◽  
Ristocetin Cofactor ◽  
Ethylenediamine Tetraacetate

Cryoprecipitates of fresh human plasma were fractionated by gel filtration on Sepharose CL-2B. Factor VIII was eluted in the void volume together with a non-proteolytic enzyme which was capable of degrading factor VIII into smaller subunits. Similar subunits were observed following treatment of factor VIII with a triglyceride lipase from Rhizopus arrhizus. They retained full functional activity (procoagulant and ristocetin cofactor). The subunits reaggregated spontaneously at 37° into a reconstituted complex which remained functionally fully active. The resulting aggregate could be repeatedly dissociated by addition of fresh lipase. The reaggregation process was enhanced by phenylmethylsulfonyl fluoride or ethylenediamine tetraacetate, but was inhibited at 0°. The treatment with lipase renders factor VIII more susceptible towards plasmin which destroys its functional properties.

scholarly journals THE ENHANCEMENT OF CHLOROFORM-INDUCED PLASMA PROTEOLYTIC ACTIVITY BY EPSILON AMINOCAPROIC ACID

1962 ◽  
Vol 115 (4) ◽  
pp. 695-706 ◽  
Author(s):  
Virginia H. Donaldson ◽  
Oscar D. Ratnoff
Keyword(s):  
Ionic Strength ◽  
Proteolytic Activity ◽  
Fibrinolytic Activity ◽  
Proteolytic Enzyme ◽  
Aminocaproic Acid ◽  
Heat Stability ◽  
Hydrolytic Activity ◽  
Casein Hydrolysis ◽  
Epsilon Aminocaproic Acid ◽  
Optimal Ph

The proteolytic activity in chloroform-treated plasma euglobulins has been attributed to plasmin. Plasmin can digest both casein and fibrin. Epsilon aminocaproic acid, which inhibits the activation of plasminogen, the precursor of plasmin, by streptokinase, urokinase, and tissue activators enhanced the development of casein hydrolytic activity in a mixture of chloroform and plasma euglobulins. Fibrinolytic activity was also enhanced, but this was evident only if the epsilon aminocaproic acid was removed from the chloroform-treated euglobulins prior to assay. The reasons for the paradoxical enhancement of chloroform-induced casein hydrolysis by euglobulins containing epsilon aminocaproic acid are unclear. However, studies of optimal pH, heat stability, and the effect of ionic strength on the activation of the precursor of this proteolytic enzyme do not differentiate it from plasminogen.

Growth and proteinase production inPseudomonasspp. cultivated under various conditions of temperature and nutrition

1968 ◽  
Vol 35 (3) ◽  
pp. 385-393 ◽  
Author(s):  
H. S. Juffs ◽  
A. C. Hayward ◽  
H. W. Doelle
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Organic Nitrogen ◽  
Proteolytic Enzymes ◽  
Dry Weight ◽  
Growth Cycle ◽  
Logarithmic Phase ◽  
Proteinase Production

SummaryA study was made of the formation of the extracellular proteolytic enzymes during the growth cycle of several species ofPseudomonascultivated under different conditions of temperature and nutrition. Proteolytic activity was not proportional to growth. Expressed per unit of cell dry weight, the proteolytic activity showed a peak in the early logarithmic phase which was greater in cultures grown at 3 than at 28°C. Proteolytic enzyme was not formed in the absence of organic nitrogen. Of 16 organisms studied,Pseudomonas aeruginosaATCC 10145 was the most prolific producer of proteolytic enzyme.

scholarly journals STUDIES ON A PROTEOLYTIC ENZYME IN HUMAN PLASMA

1952 ◽  
Vol 96 (4) ◽  
pp. 319-329 ◽  
Author(s):  
Oscar D. Ratnoff ◽  
Keyword(s):  
Human Plasma ◽  
Calcium Ions ◽  
Proteolytic Enzyme ◽  
Biological Significance ◽  
Globulin Fraction

Calcium ions accelerated the activation of the proteolytic enzyme of plasma from its precursor in the globulin fraction. Calcium did not appear to potentiate fibrinolysis by active bovine or human plasma proteolytic enzyme, nor did it accelerate the activation of the precursor of this enzyme by chloroform or by streptokinase. Experiments with partially purified plasma proteolytic enzyme suggested that the acceleratory effect of calcium was mediated indirectly. Since the concentration of calcium which was effective was comparable to that present in plasma, it is possible that the phenomena reported are of biological significance.

In Vitro Studies on a Proteolytic Enzyme from Aspergillus Oryzae (Protease I)

1968 ◽  
Vol 19 (01/02) ◽  
pp. 136-144 ◽  
Author(s):  
D Ogston ◽  
C. M Ogston
Keyword(s):  
Proteolytic Activity ◽  
Fibrinolytic Activity ◽  
Proteolytic Enzyme ◽  
Thrombolytic Agent ◽  
Inhibitory Effect ◽  
In Vitro Studies ◽  
Clotting Time ◽  
Proteolytic Action ◽  
Fibrinolytic Action

Summary1. Protease I was found to have potent fibrinolytic activity in concentrations which exceeded the blood inhibitory capacity when tested on fibrin plates and artificial thrombi.2. Plasma inhibited the proteolytic activity of protease I to a greater extent than serum; serum had a greater inhibitory effect on protease I than on plasmin. Trasylol did not inhibit the proteolytic action of protease I.3. Protease I caused the slow formation of fibrin in plasma in concentrations which did not produce fibrinogenolysis; this effect was seen in Al(OH)3-adsorbed plasma, and was not inhibited by heparin. Protease I also shortened the recalcified plasma clotting time.4. The fibrinogenolytic action of protease I was more rapid than its fibrinolytic action both in the presence and absence of plasma inhibitors. No concentration of protease I lysed fibrin in plasma without prior destruction or conversion to fibrin of the surrounding plasma fibrinogen.5. It is concluded from these in vitro studies that protease I does not have the properties necessary for a satisfactory thrombolytic agent.

Effect of trauma on rat serum proteolytic activity

1963 ◽  
Vol 204 (3) ◽  
pp. 405-407 ◽  
Author(s):  
E. Letitia Beard ◽  
John K. Hampton
Keyword(s):  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Mean Value ◽  
Serum Samples ◽  
Rat Serum ◽  
Arterial Blood ◽  
The Mean

The effect of Noble-Collip drum trauma on serum proteolytic activity of normal and trauma-resistant rats has been investigated. Rats were subjected to a range of 0–480 Noble-Collip drum revolutions (40 rev/min). Rat serum samples from arterial blood were assayed in terms of their ability to lyse casein-I131. This analysis reflected serum proteolytic enzyme (plasmin) concentration. Intensive trauma (240 revolutions and above) produced statistically significant increases in serum proteolytic activity in nonadapted and trauma-resistant rats. The level of serum proteolytic activity for both rat groups rose progressively with each increase in trauma dose. In this drumming range, (240–480 revolutions) the mean serum proteolytic activity of the nonadapted rats was consistently higher than the corresponding mean value for trauma-resistant rats at each trauma dose. It was concluded that the ability of rats to limit the production of serum proteolytic activity in response to trauma may be associated with their resistance to trauma.

scholarly journals Proteolytic Enzyme Production by Strains of the Insect Pathogen Xenorhabdus and Characterization of an Early-Log-Phase-Secreted Protease as a Potential Virulence Factor

2010 ◽  
Vol 76 (20) ◽  
pp. 6901-6909 ◽  
Author(s):  
Mustafa K. Massaoud ◽  
Judit Marokh�zi ◽  
Andr�s Fodor ◽  
Istv�n Venekei
Keyword(s):  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Galleria Mellonella ◽  
Proteolytic Enzymes ◽  
Detection Methods ◽  
Logarithmic Phase ◽  
Bacterial Strains ◽  
Native Page ◽  
Protease B

ABSTRACT As a comparison to a similar study on Photorhabdus strains, 15 Xenorhabdus bacterial strains and secondary phenotypic variants of two strains were screened for proteolytic activity by five detection methods. Although the number and intensity of proteolytic activities were different, every strain was positive for proteolytic activity by several tests. Zymography following native PAGE detected two groups of activities with different substrate affinities and a higher and lower electrophoretic mobility that were distinguished as activity 1 and 2, respectively. Zymography following SDS-PAGE resolved three activities, which were provisionally named proteases A, B, and C. Only protease B, an ∼55-kDa enzyme, was produced by every strain. This enzyme exhibited higher affinity to the gelatin substrate than to the casein substrate. Of the chromogenic substrates used, three were hydrolyzed: furylacryloyl-Ala-Leu-Val-Tyr (Fua-ALVY), Fua-LGPA (LGPA is Leu-Gly-Pro-Ala) (a substrate for collagen peptidases), and succinyl-Ala-Ala-Pro-Phe-thiobenzyl (Succ-AAPF-SBzl). All but the Fua-LGPA-ase activity seemed to be from secreted enzymes. According to their substrate preference profiles and inhibitor sensitivities, at least six such proteolytic enzymes could be distinguished in the culture medium of Xenorhabdus strains. The proteolytic enzyme that was secreted the earliest, protease B and the Succ-AAPF-SBzl-hydrolyzing enzyme, appeared from the early logarithmic phase of growth. Protease B could also be detected in the hemolymph of Xenorhabdus-infected Galleria mellonella larvae from 15 h postinfection. The purified protease B hydrolyzed in vitro seven proteins in the hemolymph of Manduca sexta that were also cleaved by PrtA peptidase from Photorhabdus. The N-terminal sequence of protease B showed similarity to a 55-kDa serralysin type metalloprotease in Xenorhabdus nematophila, which had been identified as an orthologue of Photorhabdus PrtA peptidase.

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