Resialylation of sialidase-treated sheep and human erythrocytes by Trypanosoma cruzi trans-sialidase: restoration of complement resistance of desialylated sheep erythrocytes

The initial rate of oxygen uptake by hemoglobin in sheep erythrocytes, measured within 3 hr of blood collection, was found to be considerably higher than values previously observed. No similar effect was observed with carbon monoxide unless oxygen was also present. A decay curve of the initial rate with time, obtained on human erythrocytes, indicates that the cells reach a passive level within 2 hr in the absence of oxygen. The process is inhibited by NaF and no advantage was obtained on suspending the cells in their own plasma, rather than Ringer-Locke solution. An analysis of the results suggests that the membrane is increased by cell metabolism. Submitted on September 21, 1961

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STUDIES OF THE HEMOLYSIS OF RED BLOOD CELLS BY MUMPS VIRUS

Journal of Experimental Medicine ◽

10.1084/jem.110.1.93 ◽

1959 ◽

Vol 110 (1) ◽

pp. 93-102 ◽

Cited By ~ 14

Author(s):

David W. Soule ◽

Guido V. Marinetti ◽

Herbert R. Morgan

Keyword(s):

Amniotic Fluid ◽

Red Blood Cells ◽

Blood Cells ◽

Mumps Virus ◽

Human Erythrocytes ◽

Chick Embryos ◽

Red Cell ◽

Sheep Erythrocytes ◽

Hemolytic Action ◽

Hemolytic Property

Hemolysis of chicken red blood cells by mumps virus is associated with the release of sphingomyelin from the stromal lipoprotein and the destruction of 65 per cent of the sphingomyelin of the red cell stroma. However, the virus had no effect on isolated phosphatides extracted from the erythrocytes. The hemolytic action of the virus and changes in sphingomyelin content of the erythrocytes fail to occur at a pH of 6.0. The viral hemolysis of human erythrocytes is not associated with similar alterations in their content of sphingomyelin. The absence of lecithin from sheep erythrocytes, which are also lysed by mumps virus, is additional evidence that a viral lecithinase is not associated with the hemolytic property of mumps virus. Mumps virus concentrated from the amniotic fluid of viral infected chick embryos contains about 7 per cent phosphatide, 60 per cent of which is sphingomyelin.

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Serologic Relationship of Old Tuberculin-sensitized Sheep Erythrocytes and Trypsinized Human Erythrocytes,

American Review of Tuberculosis and Pulmonary Diseases ◽

10.1164/artpd.1959.79.5.622 ◽

1959 ◽

Vol 79 (5) ◽

pp. 622-630

Author(s):

Edwin V. Buehler ◽

Melvin S. Rheins

Keyword(s):

Human Erythrocytes ◽

Sheep Erythrocytes ◽

Relationship Of

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Nucleoside transport in human and sheep erythrocytes. Evidence that nitrobenzylthioinosine binds specifically to functional nucleoside-transport sites

Biochemical Journal ◽

10.1042/bj1900377 ◽

1980 ◽

Vol 190 (2) ◽

pp. 377-383 ◽

Cited By ~ 102

Author(s):

S M Jarvis ◽

J D Young

Keyword(s):

Transport System ◽

Binding Sites ◽

Sheep Erythrocyte ◽

Specific Interaction ◽

Human Erythrocytes ◽

Nucleoside Transport ◽

Erythrocyte Membranes ◽

Sheep Erythrocytes ◽

High Affinity ◽

Transport Site

Nitrobenzyl[35S]thioinosine binding and nitro[3H]benzylthioinosine binding to nucleoside-permeable and nucleoside-impermeable sheep erythrocyte membranes was investigated, and compared with that found for human erythrocytes. High-affinity nitrobenzylthioinosine-binding sites (apparent KD congruent to 1 nM) were present on human and nucleoside-permeable but not nucleoside-impermeable sheep erythrocyte membranes (8400 and 18 sites/cell for human and sheep nucleoside-permeable sheep erythrocytes was displaced by nitrobenzylthioguanosine and dipyridamole. Uridine, inosine and adenosine inhibited binding. The smaller number of nitrobenzylthioinosine sites on nucleoside-permeable cells compared with human erythrocytes corresponded to a considerably lower Vmax. for uridine influx in these cells (0.53 × 10(-20) mol/cell per s at 25 degrees C compared with 254 × 10(-20) mol/cell per s). It is suggested that high-affinity nitrobenzylthioinosine binding represents a specific interaction with functional nucleoside-transport sites. The uridine-translocation capacity for each transport site at 25 degrees C is 180 molecules/site per s for both nucleoside-permeable sheep cells and human erythrocytes (assuming a 1:1 interaction between nitrobenzylthioinosine and the nucleoside-transport system).

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Trypanosoma cruzi: identification of a galactose-binding protein that binds to cell surface of human erythrocytes and is involved in cell invasion by the parasite

Experimental Parasitology ◽

10.1016/s0014-4894(02)00013-9 ◽

2002 ◽

Vol 100 (4) ◽

pp. 217-225 ◽

Cited By ~ 14

Author(s):

A.M Silber ◽

I.S Marcipar ◽

C Roodveldt ◽

P Cabeza Meckert ◽

R Laguens ◽

...

Keyword(s):

Cell Surface ◽

Trypanosoma Cruzi ◽

Cell Invasion ◽

Binding Protein ◽

Human Erythrocytes

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Elemental analysis of human erythrocytes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010015318x ◽

1989 ◽

Vol 47 ◽

pp. 242-243

Author(s):

S. A. Livesey ◽

A. A. del Campo ◽

E. S. Griffey ◽

D. Ohlmer ◽

T. Schifani ◽

...

Keyword(s):

Sample Preparation ◽

Elemental Analysis ◽

Human Erythrocyte ◽

Spectroscopic Analysis ◽

Model System ◽

Human Erythrocytes ◽

List Type ◽

Chemical Fixation ◽

Ethanol Dehydration ◽

Lowicryl K4m

The aim of this study is to compare methods of sample preparation for elemental analysis. The model system which is used is the human erythrocyte. Energy dispersive spectroscopic analysis has been previously reported for cryofixed and cryosectioned erythrocytes. Such work represents the reference point for this study. The use of plastic embedded samples for elemental analysis has also been documented. The work which is presented here is based on human erythrocytes which have been either chemically fixed and embedded or cryofixed and subsequently processed by a variety of techniques which culminated in plastic embedded samples.Heparinized and washed erythrocytes were prepared by the following methods for this study :(1). Chemical fixation in 4% paraformaldehyde/0.25% glutaraldehyde/0.2 M sucrose in 0.1 M Na cacodylate, pH 7.3 for 30 min, followed by ethanol dehydration, infiltration and embedding in Lowicryl K4M at -20° C.

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