scholarly journals Haemolysis induced by tyrosine crystals: Modifiers and inhibitors

1976 ◽  
Vol 158 (1) ◽  
pp. 17-22 ◽  
Author(s):  
L A Goldsmith
Keyword(s):  
Polyethylene Glycol ◽  
Human Erythrocyte ◽  
Ionic Detergents ◽  
Erythrocyte Haemolysis

Tyrosine as a solid, but not in solution, caused human erythrocyte haemolysis. Haemolysis was increased with higher tyrosine concentrations and extended incubation times; it was greater at 37degrees than 4degreesC, and decreased by higher erythrocyte concentrations. Titration of phenolic groups on the surface of di-iodotyrosine crystals altered the extent of di-iodotyrosine-induced haemolysis. Haemolysis induced by tyrosine was inhibited by polyethylene glycol (mol.wt. 6000 or 20000) in a competitive fashion; polyoxyethylene/polyoxypropylene non-ionic detergents, polyvinylpyrrolidone (mol.wt. 40000 or 360000), 0.25-1.0M-NaC1, 0.25-1.0 M-KC1 and 0.25 M-NaSCN also inhibited haemolysis. H+-ion donation from the phenolic groups of tyrosine is suggested as part of the mechanism of haemolysis. Non-ionic detergents may inhibit tyrosine-crystal-induced haemolysis by binding the phenolic groups at the surface of the crystal.

scholarly journals Some observations on the choice of detergent for solubilization of the human erythrocyte membrane

1977 ◽  
Vol 164 (2) ◽  
pp. 465-468 ◽  
Author(s):  
D A W Grant ◽  
S Hjertén
Keyword(s):  
Erythrocyte Membrane ◽  
Sodium Dodecyl Sulphate ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Human Erythrocyte Membrane ◽  
Ionic Detergents ◽  
Triton X

Solubilization of the human erythrocyte membrane by seven detergents is described. Components released into the supernatant or retained in the residue were identified by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Two non-ionic detergents exhibiting little u.v. absorption were more efficient than u.v.-absorbing Triton X-100. Evidence is presented of an interchange between protein PAS 1 and protein PAS 2.

Role of spectrin in membrane fusion and in shape change of human erythrocyte ghost

1978 ◽  
Vol 36 (2) ◽  
pp. 328-329
Author(s):  
Hideo Hayashi ◽  
Yoshikazu Hirai ◽  
John T. Penniston
Keyword(s):  
Conformational Changes ◽  
Human Erythrocyte ◽  
Shape Change ◽  
Membrane Surface ◽  
Slight Modification ◽  
Active Role ◽  
Main Role ◽  
Bank Blood ◽  
Human Erythrocyte Ghost

Spectrin is a membrane associated protein most of which properties have been tentatively elucidated. A main role of the protein has been assumed to give a supporting structure to inside of the membrane. As reported previously, however, the isolated spectrin molecule underwent self assemble to form such as fibrous, meshwork, dispersed or aggregated arrangements depending upon the buffer suspended and was suggested to play an active role in the membrane conformational changes. In this study, the role of spectrin and actin was examined in terms of the molecular arrangements on the erythrocyte membrane surface with correlation to the functional states of the ghosts.Human erythrocyte ghosts were prepared from either freshly drawn or stocked bank blood by the method of Dodge et al with a slight modification as described before. Anti-spectrin antibody was raised against rabbit by injection of purified spectrin and partially purified.

Immunocytochemical detection of hepatic carbohydrate metabolic enzymes: Improved resolution with polyethylene glycol embedding and visio-bond semithin sections

1992 ◽  
Vol 50 (1) ◽  
pp. 792-793
Author(s):  
Kuixiong Gao ◽  
Randal E. Morris ◽  
Bruce F. Giffin ◽  
Robert R. Cardell
Keyword(s):  
Polyethylene Glycol ◽  
Glycogen Phosphorylase ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Glycogen Synthase ◽  
Metabolic Enzymes ◽  
Silver Stain ◽  
Accurate Localization ◽  
Immunocytochemical Detection ◽  
Semithin Sections ◽  
Parenchymal Cells

Several enzymes are involved in the regulation of anabolic and catabolic pathways of carbohydrate metabolism in liver parenchymal cells. The lobular distribution of glycogen synthase (GS), phosphoenolpyruvate carboxykinase (PEPCK) and glycogen phosphorylase (GP) was studied by immunocytochemistry using cryosections of normal fed and fasted rat liver. Since sections of tissue embedded in polyethylene glycol (PEG) show good morphological preservation and increased detectability for immunocytochemical localization of antigenic sites, and semithin sections of Visio-Bond (VB) embedded tissue provide higher resolution of cellular structure, we applied these techniques and immunogold-silver stain (IGSS) for a more accurate localization of hepatic carbohydrate metabolic enzymes.

Directional observation on lipid of male nectary of Lindera megaphylla hemsl. by the rapid embedding method with polyethylene glycol (PEG)

1990 ◽  
Vol 48 (3) ◽  
pp. 718-719
Author(s):  
Dai Dalin ◽  
Guo Jianmin
Keyword(s):  
Electron Microscope ◽  
Polyethylene Glycol ◽  
Chemical Reaction ◽  
Traditional Method ◽  
Osmium Tetroxide ◽  
Unsaturated Lipid ◽  
Embedding Method ◽  
Long Period ◽  
New Methods

Lipid cytochemistry has not yet advanced far at the EM level. A major problem has been the loss of lipid during dehydration and embedding. Although the adoption of glutaraldehyde and osmium tetroxide accelerate the chemical reaction of lipid and osmium tetroxide can react on the double bouds of unsaturated lipid to from the osmium black, osmium tetroxide can be reduced in saturated lipid and subsequently some of unsaturated lipid are lost during dehydration. In order to reduce the loss of lipid by traditional method, some researchers adopted a few new methods, such as the change of embedding procedure and the adoption of new embedding media, to solve the problem. In a sense, these new methods are effective. They, however, usually require a long period of preparation. In this paper, we do research on the fiora nectary strucure of lauraceae by the rapid-embedding method wwith PEG under electron microscope and attempt to find a better method to solve the problem mentioned above.

Elemental analysis of human erythrocytes

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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