scholarly journals Absence of two membrane proteins containing extracellular thiol groups in Rhnull human erythrocytes

1983 ◽  
Vol 213 (1) ◽  
pp. 267-269 ◽  
Author(s):  
K Ridgwell ◽  
S J Roberts ◽  
M J A Tanner ◽  
D J Anstee
Keyword(s):  
Monoclonal Antibody ◽  
Human Erythrocyte ◽  
Osmotic Fragility ◽  
Thiol Group ◽  
Human Erythrocytes ◽  
Blood Group System ◽  
Thiol Groups ◽  
Rhesus Blood Group ◽  
Rhesus Blood Group System ◽  
Membrane Components

Rhnull human erythrocytes lack all the antigens of the Rhesus blood-group system and are associated with mild chronic haemolytic anaemia. These erythrocytes have an abnormal shape and increased osmotic fragility. Labelling studies with the impermeant maleimide N-maleoylmethionine [35S]sulphone show that Rhnull erythrocytes lack two extracellular thiol-group-containing membrane components of apparent mol.wts. 32 000 and 34 000. Immunoprecipitation with mouse monoclonal antibody R6A (which reacts with all normal erythrocytes, but fails to react with Rhnull erythrocytes) specifically precipitates the 34 000-mol.wt. component from normal erythrocytes. Similar studies with human anti-Rh(D) serum shows that this antibody reacts with the 32 000-mol.wt. component. The results suggest that the R6A-binding polypeptide and the Rh(D) polypeptide may be involved in the maintenance of the shape and viability of the human erythrocyte.

scholarly journals Identification and partial characterization of the human erythrocyte membrane component(s) that express the antigens of the LW blood-group system

1986 ◽  
Vol 234 (3) ◽  
pp. 649-652 ◽  
Author(s):  
G Mallinson ◽  
P G Martin ◽  
D J Anstee ◽  
M J A Tanner ◽  
A H Merry ◽  
...  
Keyword(s):  
Blood Group ◽  
Polyacrylamide Gel Electrophoresis ◽  
Broad Band ◽  
Osmotic Fragility ◽  
Human Erythrocytes ◽  
Blood Group System ◽  
Group System ◽  
Normal Human ◽  
Rhesus Blood Group ◽  
Rhesus Blood Group System

Rhnull human erythrocytes lack the antigens of the Rhesus blood-group system, have an abnormal shape, have an increased osmotic fragility, and are associated with mild chronic haemolytic anaemia. Rhnull erythrocytes also lack all antigens of the LW blood-group system, but the functional significance of this deficiency is unknown. We have identified, by immunoblotting with two mouse monoclonal antibodies (BS46 and BS56), the LW-active component(s) in normal human erythrocytes as a broad band of Mr 37 000-47 000 on SDS/polyacrylamide-gel electrophoresis. Treatment of intact human erythrocytes with endoglycosidase F preparation destroyed the epitopes recognized by antibodies BS46 and BS56, suggesting that one or more N-glycosidically linked oligosaccharides are required for the formation of the LW antigens. Estimation of the number of LW antigen sites per erythrocyte by using radioiodinated purified antibody BS46 gave average values of 4400 molecules/cell for Rh(D)-positive adult erythrocytes and 2835 molecules/cell for Rh(D)-negative adult erythrocytes. Like the Rh(D) polypeptide, the LW polypeptide(s) is (are) associated with the cytoskeleton of normal erythrocytes. These results suggest the possibility that the absence of the LW polypeptide may also contribute to the functional and/or morphological abnormalities of Rhnull erythrocytes.

scholarly journals Rhnull human erythrocytes have an abnormal membrane phospholipid organization

1984 ◽  
Vol 221 (3) ◽  
pp. 931-934 ◽  
Author(s):  
F Kuypers ◽  
M van Linde-Sibenius-Trip ◽  
B Roelofsen ◽  
M J Tanner ◽  
D J Anstee ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Blood Group ◽  
Haemolytic Anaemia ◽  
Osmotic Fragility ◽  
Membrane Skeleton ◽  
Human Erythrocytes ◽  
Asymmetric Distribution ◽  
Blood Group System ◽  
Rhesus Blood Group ◽  
Rhesus Blood Group System

Rhnull human erythrocytes lack the antigens of the Rhesus blood group system, have an abnormal shape and an increased osmotic fragility, and are associated with mild chronic haemolytic anaemia. Studies with phospholipase A2 and sphingomyelinase C show that the asymmetric distribution of phosphatidylethanolamine (PtdEtn) in the membrane of these cells differs from that found in control cells. The amount of PtdEtn which can be hydrolysed by phospholipase A2 in the presence of sphingomyelinase C in intact Rhnull cells is twice as high as that in normal erythrocytes. In intact Rhnull cells all of the phosphatidylcholine (PtdCho) present in the membrane can be readily exchanged with a PtdCho-specific exchange protein, whereas in control cells 75% is readily exchanged and 25% at a much lower rate. This indicates that PtdCho experiences a relatively fast transbilayer movement in the Rhnull cells. The observation that the loss of two membrane polypeptides in the Rhnull cells leads to abnormal shape, increased osmotic fragility, abnormal PtdEtn distribution and enhanced transbilayer mobility of PtdCho strongly suggests that one or both polypeptides are essential for the maintenance of a proper membrane-membrane skeleton interaction.

scholarly journals Analysis of Receptor for Vibrio choleraeEl Tor Hemolysin with a Monoclonal Antibody That Recognizes Glycophorin B of Human Erythrocyte Membrane

1999 ◽  
Vol 67 (10) ◽  
pp. 5332-5337 ◽  
Author(s):  
Dongyan Zhang ◽  
Junko Takahashi ◽  
Taiko Seno ◽  
Yoshihiko Tani ◽  
Takeshi Honda
Keyword(s):  
Monoclonal Antibody ◽  
Vibrio Cholerae ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Mammalian Cells ◽  
Biochemical Characterization ◽  
Human Erythrocytes ◽  
Human Erythrocyte Membrane ◽  
El Tor ◽  
Glycophorin B

ABSTRACT El Tor hemolysin (ETH), a pore-forming toxin secreted byVibrio cholerae O1 biotype El Tor and most Vibrio cholerae non-O1 isolates, is able to lyse erythrocytes and other mammalian cells. To study the receptor for this toxin or the related molecule(s) on erythrocyte, we first isolated a monoclonal antibody, B1, against human erythrocyte membrane, which not only blocks the binding of ETH to human erythrocyte but also inhibits the hemolytic activity of ETH. Biochemical characterization and immunoblotting revealed that this antibody recognized an epitope on the extracellular domain of glycophorin B, a sialoglycoprotein of erythrocyte membrane. Erythrocytes lacking glycophorin B but not glycophorin A were less sensitive to the toxin than were normal human erythrocytes. These results indicate that glycophorin B is a receptor for ETH or at least an associated molecule of the receptor for ETH on human erythrocytes.

scholarly journals Genetic Analysis of ABO and Rh Blood Groups in Backward Caste Population of Uttar Pradesh, India

2011 ◽  
Vol 3 (3) ◽  
pp. 07-14 ◽  
Author(s):  
Vandana RAI ◽  
Pradeep KUMAR
Keyword(s):  
Blood Group ◽  
Uttar Pradesh ◽  
Blood Groups ◽  
Blood Type ◽  
Allele Frequency Distribution ◽  
Blood Group System ◽  
Blood Group Antigens ◽  
Group System ◽  
Rhesus Blood Group ◽  
Rhesus Blood Group System

A series of glycoproteins and glycolipids on red blood cell surface constitute blood group antigens. These are AB, A, B and O in ABO blood group system and Rh in rhesus blood group system. A total of 1065 unrelated Backward Caste (OBC) individuals from Uttar Pradesh were studied for the phenotype and allele frequency distribution of ABO and Rh (D) blood groups. Total 1065 samples analyzed, phenotype B blood type has the highest frequency 36.81% (n=392), followed by O (32.68%; n=348), A (23.66%; n=252) and AB (6.85%; n=73). The overall phenotypic frequencies of ABO blood groups were B>O>A>AB. The allelic frequencies of O, A, and B alleles were 0.5819, 0.1674 and 0.2506 respectively. Out of total 1065 samples, 1018 (95.59%) samples were Rh-positive and 47 (4.41%) were Rh-negative. Phenotypic frequency of Rh-negative in Koari, Yadav, Kurmi and Maurya samples were 0.99%, 4%, 1.4% and 7.6% respectively.

BLOOD GROUP PROBABILITIES BY NEXT OF KIN

2018 ◽  
Vol 34 (3) ◽  
pp. 343-363
Author(s):  
Joost H. J. van Sambeeck ◽  
Nico M. van Dijk ◽  
Wim L. A. M. de Kort ◽  
Henk Schonewille ◽  
Mart P. Janssen
Keyword(s):  
Blood Group ◽  
Mathematical Formulation ◽  
Blood Groups ◽  
Point Of View ◽  
Blood Group System ◽  
Genotype Distribution ◽  
Next Of Kin ◽  
Quadratic Stochastic Operators ◽  
Rhesus Blood Group ◽  
Rhesus Blood Group System

For rare blood groups the recruitment of donor relatives, for example siblings, is expected to be effective, since the probability of a similar rare blood group is likely. However, the likelihood differs between blood groups and is not commonly available. This paper provides a unified mathematical formulation to calculate such likelihoods. From a mathematical and probabilistic point of view, it is shown that these likelihoods can be obtained from the computation of a stationary genotype distribution. This, in turn, can be brought down to a system of quadratic stochastic operators. A generic mathematical approach is presented which directly leads to a stationary genotype distribution for arbitrary blood groups. The approach enables an exact computation for the effectiveness of recruiting next of kin for blood donorship. Next to an illustration of computations for ‘standard’ ABO and Rhesus-D blood groups, it is particularly illustrated for the extended Rhesus blood group system. Also other applications requiring next of kin blood group associations can be solved directly by using the unified mathematical formulation.

Seed Agglutinin with Specificity within the Rhesus Blood Group System

Nature ◽  
1968 ◽  
Vol 219 (5154) ◽  
pp. 653-653 ◽  
Author(s):  
G. W. G. BIRD ◽  
JUNE WINGHAM
Keyword(s):  
Blood Group ◽  
Blood Group System ◽  
Group System ◽  
Rhesus Blood Group ◽  
Rhesus Blood Group System
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