ABSORPTION OF ULTRASOUND IN HUMAN BLOOD

1990 ◽  
Vol 51 (C2) ◽  
pp. C2-311-C2-314
Author(s):  
G. GOPALA KRISHNA ◽  
A. K.W. ANWAR ALI ◽  
A. AHMAD
Keyword(s):  
Human Blood

α-Linoleic acid enhances the capacity of α1-antitrypsin to inhibit lipopolysaccharide-induced IL-1β in human blood neutrophils

Pneumologie ◽  
2016 ◽  
Vol 70 (07) ◽  
Author(s):  
N Aggarwal ◽  
S Wrenger ◽  
V Grau ◽  
T Welte ◽  
S Janciauskiene
Keyword(s):  
Linoleic Acid ◽  
Human Blood ◽  
Blood Neutrophils

Fibrinogen-Fibrin-Related Antigen Pattern in Human Blood

1974 ◽  
Vol 32 (02/03) ◽  
pp. 266-276
Author(s):  
Carl D. Jacobsen ◽  
John C. Hoak ◽  
Kenneth K. WU ◽  
Glenna L. Fry
Keyword(s):  
Human Blood ◽  
Plasma Samples

SummaryIn serum from patients with DIC at least 3 different FR-antigenic components could be found. It was difficult to demonstrate these components in the corresponding plasma samples. It is possible that a portion of these antigens formed as a result of in vitro clotting despite the presence of proteolytic inhibitors. These results suggest that the interpretation of “increased split products in serum” may be more complex than current concepts indicate.

On the Mechanism by which Cell Contact Induces the Release Reaction of Blood Platelets; the Effect of Cationic Polymers

1972 ◽  
Vol 27 (01) ◽  
pp. 121-133 ◽  
Author(s):  
P Massini ◽  
E. F Lüscher
Keyword(s):  
Human Blood ◽  
Calcium Ions ◽  
Blood Platelets ◽  
Cell Contact ◽  
Second Phase ◽  
Cationic Polymers ◽  
Release Reaction ◽  
Per Se ◽  
Human Blood Platelets

SummaryHuman blood platelets are aggregated by the basic polymers polylysine and DEAE- dextran. Under certain conditions a second phase of aggregation, concomitant with the release reaction, is elicited. The presence of ADP, calcium ions and a plasmatic cofactor within the primary aggregates are necessary for the induction of the release reaction. These experiments demonstrate that cell contact per se does not lead to a release reaction ; in order to become effective it must take place in the presence of ADP.

Effect of Aspirin on the Thrombelastogram of Human Blood

1973 ◽  
Vol 30 (03) ◽  
pp. 494-498 ◽  
Author(s):  
G de Gaetano ◽  
J Vermylen
Keyword(s):  
Oral Dose ◽  
Single Oral Dose ◽  
Platelet Function ◽  
Human Blood ◽  
Platelet Rich Plasma ◽  
Plasma Samples ◽  
Release Reaction ◽  
Platelet Release

SummaryThrombelastograms of both native blood and re-calcified platelet-rich plasma samples taken from subjects given a single oral dose of aspirin (1 gram) were not significantly different from the pretreatment recordings. Aspirin also did not modify the thrombelastogram when preincubated in vitro with platelet-rich plasma at concentrations inhibiting the platelet “release reaction” by collagen. Thrombelastography therefore cannot evaluate the effect of aspirin on platelet function.

The Effect of Dipyridamole and RA 233 on Human Platelet Function in Vitro

1973 ◽  
Vol 29 (03) ◽  
pp. 694-700 ◽  
Author(s):  
Paul L. Rifkin ◽  
Marjorie B. Zucker
Keyword(s):  
Mechanism Of Action ◽  
Human Blood ◽  
Glass Bead ◽  
Heart Valves ◽  
Human Platelet ◽  
Drug Effects ◽  
Simple Relation ◽  
Prosthetic Heart Valves ◽  
Induced Aggregation

SummaryDipyridamole (Persantin) is reported to prolong platelet survival and inhibit embolism in patients with prosthetic heart valves, but its mechanism of action is unknown. Fifty jxM dipyridamole failed to reduce the high percentage of platelets retained when heparinized human blood was passed through a glass bead column, but prolonged the inhibition of retention caused by disturbing blood in vitro. Possibly the prostheses act like disturbance. Although RA 233 was as effective as dipyridamole in inhibiting the return of retention, it was less effective in preventing the uptake of adenosine into erythrocytes, and more active in inhibiting ADP-induced aggregation and release. Thus there is no simple relation between these drug effects.

Chromatographic Isolation of the LDH-Isoenzymes of Human Blood Platelets and an Investigation of Their Enzyme Kinetics

1968 ◽  
Vol 20 (03/04) ◽  
pp. 301-313 ◽  
Author(s):  
W Schneider ◽  
K Schumacher ◽  
B Thiede ◽  
R Gross
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Deae Cellulose ◽  
Order Reaction ◽  
Kinetic Properties ◽  
Ldh Isoenzymes ◽  
Kinetic Investigations ◽  
Substrate Concentrations ◽  
Chromatographic Isolation ◽  
Human Blood Platelets

SummaryThe LDH-isoenzymes of human blood platelets show a distinct predominance of the isoenzymes 2 and 3 upon chromatography on DEAE-cellulose. Small amounts of LDH-1 are also present, while only traces of LDH-4 and -5 can be detected.Enzyme kinetic investigations of the principal isoenzymes LDH-1, -2 and -3 clearly show that the differences in inhibition constants with pyruvate as substrate which are demonstrable at 25° largely disappear at 37°. On the other hand, the differences among the isoenzymes in their affinity for pyruvate and lactate as substrate as well as in with respect to the optimal substrate concentrations of pyruvate are more marked at 37° than at 25°. Also, the type of inhibition found with lactate as substrate is increasingly the expression of a higher order reaction in going from LDH-1 to LDH-3. A dependence of the LDH distribution pattern upon the metabolism of the cell is discussed. A comparison of our results with thrombocytes with those of other workers with erythrocytes and leucocytes makes it unlikely that the LDH pattern is directly dependent upon the existence of an oxidative metabolism. Rather, the redox potential of the cell could be of importance for the nature of the pattern of isoenzymes and for their differing kinetic properties.

The Lysis of Artificial Thrombi

1980 ◽  
Vol 43 (01) ◽  
pp. 034-037 ◽  
Author(s):  
Michael J Metcalf
Keyword(s):  
Human Blood ◽  
Final Concentration ◽  
Rabbit Blood ◽  
Factors Influencing ◽  
Dextran 70 ◽  
Chandler Loop ◽  
Loop Technique

SummaryThe susceptibility to lysis of artificial thrombi formed from native rabbit blood in the presence or absence of dextran was determined using the Chandler loop technique. Thrombi of identical weight were formed in the presence of saline or dextran and when spontaneous thrombolysis was allowed to take place, thrombi formed in the presence of dextran 70 were lysed to a greater extent than those formed under control conditions.The possible factors influencing this observation were studied. Increasing concentrations of streptokinase increased the extent of thrombolysis in both control and dextran treated thrombi. Maximal streptokinase induced thrombolysis occurred in the presence of a 2 per cent final concentration of dextran Mw 40,000 and 500,000 and dextran 70 at a final concentration of 1.2 per cent.Increased thrombolysis was not observed when albumin was substituted for dextran.Finally, similar observations were recorded for streptokinase induced thrombolysis using human blood.

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