scholarly journals Use of pectic polysaccharides for cryopreservation of biological objects

2014 ◽  
Vol 66 (3) ◽  
pp. 1025-1033 ◽  
Author(s):  
Т.V. Polezhaeva ◽  
О.О. Zaitseva ◽  
А.N. Khudyakov ◽  
D.S. Laptev ◽  
V.V. Golovchenko ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Red Blood Cells ◽  
Human Blood ◽  
Blood Cells ◽  
Blood Platelets ◽  
Pectic Polysaccharides ◽  
Pectic Polysaccharide ◽  
Biological Objects ◽  
Human Blood Platelets

The protectant activity of pectic polysaccharides derived from various plants was studied on Saccharomyces cerevisiae yeast-like fungi, human blood platelets and leukocytes, and the antihemolytic action of the same compounds was studied on red blood cells. The feasibility of cryopreservation of biological objects in the environment of pectic polysaccharide- containing cryoprotectant solutions was demonstrated.

Adsorption of Carbon-14 Dextran to Human Blood Platelets and Red Blood Cells, in Vitro

Vox Sanguinis ◽  
1957 ◽  
Vol 2 (2) ◽  
pp. 104-109 ◽  
Author(s):  
S. ROTHMAN ◽  
E. ADELSON ◽  
A. SCHWEBEL ◽  
R. D. LANGDELL
Keyword(s):  
Red Blood Cells ◽  
Human Blood ◽  
Blood Cells ◽  
Blood Platelets ◽  
Carbon 14 ◽  
Human Blood Platelets

Adsorption of Carbon-14 Dextran to Human Blood Platelets and Red Blood Cells, in Vitro *

Vox Sanguinis ◽  
1957 ◽  
Vol 2 (2) ◽  
pp. 104-109
Author(s):  
S. Rothman ◽  
E. Adelson ◽  
A. Schwebel ◽  
R.D. Langdell ◽  
G. Fraction
Keyword(s):  
Red Blood Cells ◽  
Human Blood ◽  
Blood Cells ◽  
Blood Platelets ◽  
Carbon 14 ◽  
Human Blood Platelets

Influence of Decalcifying Agents in Increasing Concentrations on the Stability of Human Platelets

1961 ◽  
Vol 05 (03) ◽  
pp. 559-565 ◽  
Author(s):  
R Honorato ◽  
G Schindler
Keyword(s):  
Red Blood Cells ◽  
Human Blood ◽  
Blood Cells ◽  
Sodium Citrate ◽  
Blood Platelets ◽  
Human Platelets ◽  
Sodium Oxalate ◽  
Blood Samples ◽  
The Stability ◽  
Human Blood Platelets

Summary1. The influence of 0.025 M, 0.1 M, 0.2 M sodium oxalate and of 0.2 M sodium citrate on the stability of human blood platelets was studied.2. A diminution of the resistance of platelets to glass in the 0.025 M and 0.1.M sodium oxalate blood samples was observed.3. This effect of oxalate was not observed when red blood cells were not present.

The Mechanism of Platelet Aggregation in Relation to Hemostasis

1962 ◽  
Vol 07 (03) ◽  
pp. 480-490 ◽  
Author(s):  
R Käser-Glanzmann ◽  
E. F Lüscher
Keyword(s):  
Platelet Aggregation ◽  
Human Blood ◽  
Blood Cells ◽  
Blood Platelets ◽  
Molar Ratio ◽  
Human Blood Platelets

SummaryThe finding that ADP induces the aggregation of human blood platelets is confirmed. Under the influence of thrombin platelets release enough. ADP to account for their mutual aggregation during viscous metamorphosis. Other nucleotides liberated under the same conditions are ATP and AMP. The nucleotides released from platelets during VM have been separated by chromatography and a molar ratio of ATP : ADP : AMP = 1 : 5 : 3 has been found. It is concluded that platelet aggregation by ADP in the course of the formation of the hemostatic plug is a self contained process normally independent of the presence of other blood cells.

scholarly journals Interaction of Influenza Virus with Blood Platelets

Blood ◽  
1966 ◽  
Vol 28 (2) ◽  
pp. 213-228 ◽  
Author(s):  
HIDEO TERADA ◽  
MARIO BALDINI ◽  
SHIRLEY EBBE ◽  
MORTON A. MADOFF
Keyword(s):  
Influenza Virus ◽  
Human Blood ◽  
Blood Cells ◽  
Blood Platelets ◽  
Live Virus ◽  
Human Red Blood Cells ◽  
Virus Adsorption ◽  
Human Blood Platelets

Abstract The interaction of human blood platelets with influenza virus (PR-8) was studied in vitro and in vivo. It was found that "live" influenza virus was rapidly adsorbed onto human blood platelets at 4 C. and completely eluted at 37 C. "Dead" virus was adsorbed at 4 C. but not eluted at 37 C. unless the platelets were treated with RDE (receptor destroying enzyme). Adorption of virus also occurred at tem peratures above 4 C. (from 20 to 37 C.). However, while adsorption was maintained throughout incubation at 4 C., slow elution occurred after 30 to 90 minutes incubation at 26 to 37 C. Storage of the platelets for lengthy intervals at 4 C. or coating of the platelets with macromolecules did not interfere with virus adsorption. After one cycle of adsorption-elution, blood platelets could not adsorb virus again. Treatment with RDE greatly reduced virus adsorption. During the process of virus adsorption, prominent platelet clumping occurred. During elution, clumping remained unchanged, and gross alterations in morphology of the platelets were observed. In the process of virus adsorption-elution, large numbers of platelets were lysed. Comparative experiments were performed simultaneously with human red blood cells (RBC) and identical results were obtained as with blood platelets. However, the extent of adsorption of live virus was equal for platelets and RBC only when the relationship between platelet number and RBC number in the preparations used was 6:1. This suggested a direct proportion between the surface area of both platelet and RBC and the number of available virus receptors. Virus suspensions infused into rabbits produced a sharp and sustained drop of the platelet count. Survival of radioactively labeled platelets treated with virus prior to infusion was markedly shortened with live virus and was only slightly reduced with dead virus. It is suggested from these experiments that blood platelets, as other blood cells, may serve as carriers of viruses in the circulation and that in this process the platelets are damaged and partially destroyed.

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.

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.

Interaction of Vasopressin with Human Blood Platelets: Dependency on Mg2+

1986 ◽  
Vol 56 (03) ◽  
pp. 260-262 ◽  
Author(s):  
Isabella Roos ◽  
Fabrizia Ferracin ◽  
Alfred Pletscher
Keyword(s):  
Phosphatidic Acid ◽  
Human Blood ◽  
Arginine Vasopressin ◽  
Specific Binding ◽  
Blood Platelets ◽  
Bivalent Cations ◽  
Platelet Membranes ◽  
Maximal Rise ◽  
Human Blood Platelets ◽  
Stimulation Of

SummaryArginine-vasopressin (AVP) in the presence of Mg2+ but not in the absence of bivalent cations led to accumulation of [32P]-phosphatidic acid ([32P]-PA) in human blood platelets. Mg2+ also enhanced the specific binding of [3H]-AVP to intact platelets. The concentrations of the cation which enabled AVP to cause half maximal rise of [32P]-PA and those inducing half maximal [3H]-AVP-binding were of the same order. It is concluded that the stimulation of phosphatidyl inositide breakdown by AVP in presence of Mg2+ is at least partially due to a Mg2+-induced enhancement of specific AVP-binding to the platelet membranes.

Benzalkonium chloride interferes with energy production, secretion and morphology in human blood platelets

Platelets ◽  
1999 ◽  
Vol 10 (2) ◽  
pp. 97-104 ◽  
Author(s):  
Ø. Berg ◽  
A. M. Bakken ◽  
S. K. Steinsvåg ◽  
M. Farstad
Keyword(s):  
Human Blood ◽  
Benzalkonium Chloride ◽  
Energy Production ◽  
Blood Platelets ◽  
Human Blood Platelets
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