In vitro studies of the hemolytic activity of microemulsions in human erythrocytes

2005 ◽  
Vol 39 (5) ◽  
pp. 1063-1067 ◽  
Author(s):  
Rosa M. Aparicio ◽  
M. José García-Celma ◽  
M. Pilar Vinardell ◽  
Montserrat Mitjans
2017 ◽  
Author(s):  
G. Radha ◽  
Rohith Vinod K. ◽  
Balaji Venkatesan ◽  
Elangovan Vellaichamy ◽  
S. Balakumar

Blood ◽  
1960 ◽  
Vol 15 (1) ◽  
pp. 130-136 ◽  
Author(s):  
JOSEPH D. SHERMAN ◽  
CARMEN RICKARD ◽  
ROBERT S. CHRISTIAN ◽  
GILBERT H. FRIEDELL

Abstract 1. Sterile, cell-free extracts of the viable portion of a methylcholanthrene-induced sarcoma of the hamster were capable of hemolyzing in vitro hamster red blood cells from the donor animals, and from animals with homologous and heterologous tumors. 2. Sterile, cell-free extracts of the necrotic material from this same tumor had little in vitro hemolytic action. 3. Whole tumor extracts varied in their in vitro hemolytic activity depending upon the proportion of viable to necrotic tissue present, with the maximum hemolysis observed when the whole tumor contained more viable than necrotic tissue. 4. Sterile, cell-free extracts of normal hamster liver had a strong hemolytic action on a whole range of red blood cells. 5. Hemolysins elaborated by the viable tissue in transplanted hamster tumors may be one factor contributing to the anemia in hamsters bearing transplantable sarcomas.


1956 ◽  
Vol 40 (1) ◽  
pp. 121-134 ◽  
Author(s):  
Blanche Ann Borek ◽  
Max Bovarnick

1. Hemolyzed rabbit cells contain a factor which lyses human erythrocytes in vitro when Mg++ and certain nucleotides are supplied to the system. Of the nucleotides tested ATP is the most active, although no net loss of ATP or of labile phosphate seems to be associated with the hemolytic process. 2. The lytic factor appears to be a sulfhydryl enzyme which attacks the membrane of the human red cell, its hemolytic activity being inhibited by human stroma. 3. The system is activated by glutathione and is inhibited by heavy metals, oxidized glutathione, cysteine, ergothionine, and a number of metabolic inhibitors. Physostigmine has no effect. 4. Partial purification of the lytic factor has been achieved by fractional centrifugation.


2006 ◽  
Vol 15 (04) ◽  
pp. 245-257 ◽  
Author(s):  
H. J. Rolf ◽  
K. G. Wiese ◽  
H. Siggelkow ◽  
H. Schliephake ◽  
G. A. Bubernik

1968 ◽  
Vol 19 (03/04) ◽  
pp. 584-592 ◽  
Author(s):  
Hanna Lukasiewicz ◽  
S Niewiarowski

Summary and Conclusion1. It has been found that EACA does not inhibit activation of human plasminogen into plasmin by SK and UK in a concentration of 5 × 10–2 M. The activation of bovine plasminogen by SK and UK is inhibited by this concentration of EACA but not by a lower one.2. EACA in concentrations of 1,5 × 10–1 – 10–4 M does not inhibit casein proteolysis by plasmin. The proteolysis of fibrinogen and fibrin measured by the release of TCA soluble tyrosine is inhibited by EACA in concentrations of 1,5 × 10–1 – 10–2 M.3. The lysis of non-stabilized clots by plasmin measured in a test tube was inhibited by an EACA concentration of 5 × 10–3 – 5 × 10–4 M. The lysis of stabilized clots by plasmin was inhibited by an EACA concentration of 10–5 M.4. On the basis of experimental findings and data given in literature the authors postulate that the mechanism of the antifibrinolytic effects of EACA consists mainly in a modification of plasmin action on fibrin. These effects are dependent on the structure of the fibrin clots.


1969 ◽  
Vol 21 (02) ◽  
pp. 234-244 ◽  
Author(s):  
N Mackay ◽  
J.C Ferguson ◽  
Antonia Bagshawe ◽  
A.T.T Forrester ◽  
G.P Mcnicol
Keyword(s):  

SummaryAn account is given of the effects of boomslang venom in man. Evidence was found of a fibrinolytic state apparently secondary to the coagulant action of the venom. These features rapidly responded to the administration of specific antivenom. In vitro studies, using a homogenate of boomslang parotids, confirmed the coagulant properties of the venom and showed them to be of much greater potency than the proteolytic actions.


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