Antigenic Properties of Human Erythrocyte Glycophorins

1988 ◽  
pp. 265-315 ◽  
Author(s):  
Elwira Lisowska
Keyword(s):  
Human Erythrocyte ◽  
Antigenic Properties

Chemical and Antigenic Properties of a Human Erythrocyte Protein

1974 ◽  
pp. 33-38
Author(s):  
H. WEICKER ◽  
F. RITTHALER ◽  
H. SCHMID ◽  
W. EBERT ◽  
A. REINDELL ◽  
...  
Keyword(s):  
Human Erythrocyte ◽  
Antigenic Properties

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.

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.

The Immunological Properties of Factor VIII

1966 ◽  
Vol 16 (03/04) ◽  
pp. 559-573 ◽  
Author(s):  
L Uszyński
Keyword(s):  
Factor Viii ◽  
Inhibitory Activity ◽  
Hemophilia A ◽  
Severe Form ◽  
Molecular Defect ◽  
Bovine Plasma ◽  
Human Factor Viii ◽  
Antigenic Properties ◽  
Coagulation Tests ◽  
Normal Human

SummaryRabbits immunized against human AHG fibrinogen-free preparations, were shown to produce anti-AHG antibodies. The inhibitory activity of these antibodies was tested by thromboplastin generation test, thrombelastography, and the specific anti-AHG antibodies neutralization test. The latter test permitted quantitative determination of antigenic form of factor VIII. The inhibitory activity of anti-FI-O-Ta serum resulted exclusively from the anti-AHG antibodies which in coagulation tests behaved like circulating anticoagulants directed against factor VIII.The anti-AHG antibodies were neutralizable by normal human serum or plasma even contained only trace of AHG activity after storage. There was no antigenic form of factor VIII in the severely affected patients with hemophilia A, von Willebrand’s disease nor in the normal plasma adsorbed on bentonite. The presented results suggest a molecular defect of factor VIII in patients with hemophilia A. The severe form of this disease depends, probably, on a major impairment of AHG biosynthesis, leading to changes in the antigenic properties of the molecule. The AHG from rabbit, porcine and bovine plasma respectively did not neutralize the anti-AHG antibodies formed in rabbits immunized against human factor VIII preparations.

CHEMISTRY OF GONADOTROPHINS IN RELATION TO THEIR ANTIGENIC PROPERTIES

1969 ◽  
Vol 62 (1_Suppl) ◽  
pp. S13-S30 ◽  
Author(s):  
W. R. Butt
Keyword(s):  
Biological Activity ◽  
Guinea Pigs ◽  
Complement Fixation ◽  
Neuraminic Acid ◽  
Fixation Technique ◽  
Immunological Activity ◽  
Antigenic Properties ◽  
Specific Antisera ◽  
Structural Differences

ABSTRACT Several chemical differences between FSH, LH and HCG have been reported: thus LH and HCG are richer in proline than FSH and FSH and HCG contain more N-acetyl neuraminic acid than LH. Sub-units of LH are formed by treatment with urea, guanidine or acid. HCG also may contain two sub-units. The sub-units from LH are biologically inert but retain their immunological activity: biological activity is restored when the sub-units are incubated together. There is much evidence from chemical and enzymic reactions that antigenic groups are distinct from those parts of the molecule essential for biological activity. N-acetyl neuraminic acid and probably other carbohydrates in FSH and HCG are not involved in immunological activity but are necessary for biological activity. Histidine, methionine and possibly cysteine appear to be essential for biological but not immunological activity of FSH, while tryptophan and possibly tyrosine are not essential for either. A few highly specific antisera to gonadotrophins have been prepared in rabbits and guinea pigs to crude antigens: there is no evidence that purified antigens are more likely to produce specific antisera. Differences in the immunological reactivities of urinary compared with pituitary gonadotrophins have been observed both by radioimmunoassay and by the complement fixation technique. The latter may be particularly useful for detecting structural differences in the hormones.

Structure of the human erythrocyte insulin receptor

Diabetes ◽  
1986 ◽  
Vol 35 (1) ◽  
pp. 101-105 ◽  
Author(s):  
G. M. Ward ◽  
L. C. Harrison
Keyword(s):  
Insulin Receptor ◽  
Human Erythrocyte
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