Blood Group Genetics
Geoff Daniels, Bristol Institute for Transfusion Sciences Services, Bristol, UK
Blood groups are antigenic determinants on blood cells that represent inherited variation
of the proteins, glycoproteins and glycolipids that are exposed at the cell surface. Most of
the genes encoding blood group antigens, either directly or indirectly, have been cloned
and the molecular bases for many of the polymorphisms are known.
Introduction
Blood groups are antigenic determinants on the surface of
red cells, platelets and granulocytes, but the use of the term
is often restricted to antigens on red blood cells. Blood
groups are defined by antibodies, usually alloantibodies
produced by individuals who lack the corresponding
antigen. Some blood group antibodies, such as anti-A
and anti-B, are present in the plasma of everybody whose
red cells lack the corresponding antigen, but most blood
group antibodies are formed only in response to antigen-
positive red cells as the result of transfusion or pregnancy.
Almost all blood groups are inherited characters, although
some blood group phenotypes may be modified by
environment, development or disease. Some blood group
antigens are detected on only one type of blood cell, such as
the Rh antigens on red cells; others may also be present on
other blood cells and in other tissues. Those with wide
distribution throughout the body, such as the ABO
antigens, are referred to as histo-blood group antigens.
Some blood groups are carried by carbohydrate
structures on glycoproteins and glycolipids. They include
the histo-blood group antigens ABO, H and Lewis, and the
P antigens. The genes controlling their expression do not
encode the antigen directly, but produce transferase
enzymes that catalyse biosynthesis of the antigens by
stepwise addition of monosaccharide residues to an
oligosaccharide chain. However, most blood group anti-
gens are proteins or glycoproteins in which the main factor
determining the blood group polymorphism is amino acid
sequence, encoded directly by the blood group gene. With
these glycoproteins the presence of carbohydrate may still
play a role in expression of the antigen. Many blood group
polymorphisms represent single amino acid substitutions,
but some, in the more complex MNS and Rh systems,
involve a variety of different genetic mechanisms involving
intergenic recombination and splice site mutations.
The functions of some red cell antigens are known: some
antigens act as membrane transporters and channels,
facilitating the movement of biologically important
molecules in or out of the cells; some are complement
regulatory proteins, protecting the cells from attack from
autologous complement; and some have a structural
function. Functions of some antigens on red cells can be
surmised, either because their functions on other cells are
ENCYCLOPEDIA OF LIFE SCIENCES / & 2001 Nature Publishing Group / www.els.net
Introductory article
Article Contents
. Introduction
. Blood Group Classification
. Major Blood Group Systems
. Platelet and Neutrophil Antigens
known or because they resemble other structures of known
function. Almost nothing is known, however, of the
biological significance of blood group polymorphism.
Blood Group Classification
The International Society for Blood Transfusion has
devised a genetic classification for human red cell surface
antigens, based on blood group systems. A blood group
system is one or more antigens encoded by a single gene, or
by a cluster of two or more closely linked, homologous
genes. There are 25 blood group systems (Table 1): some
contain only one specificity; Rh, the largest system,
contains 45. The MNS system encompasses three genes,
the Rh and Chido/Rodgers systems two genes each, and
the remainder appear to represent single genes. The genes
controlling all the blood group systems have been located
on specific chromosomes (Table 1); the genes for all but four
(P, DO, SC, RAPH) have been cloned and sequenced. In
addition to the antigens of the blood group systems there
are about 50 other well-defined red cell antigens, mostly of
very high or very low frequency, that have not been
assigned to a system because of insufficient genetic
evidence.
Major Blood Group Systems
ABO system
ABO, the most important blood group system from the
clinical blood transfusion perspective, was discovered in
1900 by Landsteiner, the discovery that first made blood
transfusion feasible. At its basic level, there are two ABO
antigens, A and B, giving rise to four phenotypes, A, B, AB
and O. In the O phenotype, neither A nor B is produced
(Table 2). Group A people generally have anti-B in their
plasma, group B people have anti-A, group AB people
have neither antibody, and group O people have anti-A,B.
These are predominantly agglutinating immunoglobulin
(Ig) M antibodies. Anti-A,B will agglutinate group A or B
cells. In transfusion medicine it is imperative that donor red
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 Blood Group Genetics

Table 1 Blood group systems, the genes that encode them, and their chromosomal location
No. System name Systemsymbol Gene name(s) Chromosome No. of antigens
001 ABO ABO ABO 9 4
002 MNS MNS GYPA, GYPB, GYPE 4 43
003 P P1 P1 22 1
004 Rh RH RHD, RHCE 1 45
005 Lutheran LU LU 19 18
006 Kell KEL KEL 7 23
007 Lewis LE FUT3 19 6
008 Duffy FY FY 1 6
009 Kidd JK SLC14A1 18 3
010 Diego DI SLC4A1 17 18
011 Yt YT ACHE 7 2
012 Xg XG XG X 1
013 Scianna SC SC 1 3
014 Dombrock DO DO 12 5
015 Colton CO AQP1 7 3
016 Landsteiner–Wiener LW LW 19 3
017 Chido/Rodgers CH/RG C4A, C4B 6 9
018 Hh H FUT1 19 1
019 Kx XK XK X 1
020 Gerbich GE GYPC 2 7
021 Cromer CROM DAF 1 10
022 Knops KN CR1 1 5
023 Indian IN CD44 11 2
024 Ok OK CD147 19 1
025 Raph RAPH MER2 11 1

Table 2 ABO antigens, antibodies and genotypes

ABO group Antigens on red cells Antibodies in serum Genotype
O None Anti-A,B O/O
A A Anti-B A/A or A/O
B B Anti-A B/B or B/O
AB A and B None A/B

cells that are agglutinated by the patient’s plasma are not
transfused. Approximate frequencies of ABO phenotypes
in southern England are as follows: O, 43%; A, 45%; B,
8%; AB, 4%, but ABO frequencies vary throughout the
world.
The A and B determinants are carbohydrate structures,
present on some red cell membrane glycoproteins and
glycolipids. Carbohydrate chains are synthesized by the
action of glycosyltransferases, enzymes that catalyse the
transfer of specific monosaccharides from a nucleotide
donor substrate to an acceptor substrate. The acceptor
substrate for A and B transferases, products of the A and B
alleles, is a terminally fucosylated structure called H
antigen, shown in Figure 1. The A gene product is an N-
acetylgalactosaminyltransferase that transfers N-acetylga-
lactosamine from a uridine diphosphate (UDP)–N-acet-
ylgalactosamine donor substrate to the fucosylated
galactosyl residue of the H antigen, to produce an A-
active structure (Figure 1). B gene product is a galactosyl-
transferase that transfers galactose from UDP–galactose
to the fucosylated galactose of H, to produce a B-active
structure (Figure 1). The O allele produces no active
enzyme, so on group O red cells the H antigen remains
unconverted. N-acetylgalactosamine and galactose are the
immunodominant sugars of A and B blood groups
respectively.
A and B transferases are encoded by a single gene on
chromosome 9. The ABO gene spans about 18–20
kilobases (kb) organized into seven exons of coding
sequence. Exons 6 and 7, the two largest, encode 77% of

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O (H) Gal GlcNAc R A and B transferases. This H deficiency results from
Fuc
Gal GlcNAc R fucosyltransferase gene (FUT1) is responsible for produc-
A GalNAc
Fuc
Gal GlcNAc R the Bombay phenotype usually make a potent anti-H.
B Gal
Fuc
Figure 1 Diagrammatic representation of the H-active trisaccharide on
group O cells and the group A- and B-active oligosaccharides. R, remainder
of molecule; GlcNAc, N-acetylglucosamine; Gal, galactose; Fuc, fucose;
GalNAc, N-acetylgalactosamine.
the full coding region and probably all of the catalytically
active domain. The products of the A and B alleles differ by
four amino acid substitutions at residues 176, 235, 266 and
268. Amino acid residues at positions 266 and 268 are most
important in determining whether the gene product has
predominantly N-acetylgalactosaminyltransferase (A) or
galactosyltransferase (B) activity. The sequence of the
most common O allele (O1) is identical to the A sequence,
apart from a single nucleotide deletion that is responsible
for a reading frame shift after codon 86 and the generation
of a translation stop signal at codon 117. This allele
encodes a truncated protein lacking the catalytic site. There
are two other common O alleles: O1v, which, like O1, has
the single nucleotide deletion, but differs from O1 by nine
nucleotide changes within the coding sequence, and O2,
which does not have the single nucleotide deletion but is
inactivated by a missense mutation encoding a Gly268Arg
substitution.
A antigen is divided into two main subgroups, A1 and
A2. A1 and A2 (and A1B and A2B) red cells react with anti-
A, A1 cells reacting more strongly than A2 cells, but A1 cells
also react with anti-A1, an antibody present in the serum of
some A2 and A2B individuals. Thus the A antigens of A1
and A2 cells differ quantitatively and qualitatively. A2-
transferase is substantially less efficient than A1-transfer-
ase. A2 deoxyribonucleic acid (DNA) has a single base
deletion in the codon before the usual translation stop
codon, resulting in a reading frame shift and loss of the stop
codon. The protein product has an extra 21 amino acid
residues at the C-terminus, presumed to be responsible for
reduction in enzyme activity.
A and B antigens are widely distributed in the body and
are often called histo-blood group antigens. They are also
present in soluble form in body secretions. About 20% of
group A or B people secrete no A or B substance, because
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Blood Group Genetics
their secretions contain no H antigen, the substrate for the
inactivity of the fucosyltransferase that is crucial for
biosynthesis of H, due to mutations within the fucosyl-
transferase gene, FUT2. These ABH ‘nonsecretors’ have A
or B antigen on their red cells because a different
tion of H antigen on red cells. In a very rare phenotype, the
Bombay phenotype, mutations in FUT1 and FUT2 result
in no H, and consequently no A or B, on red cells or in
secretions, regardless of ABO genotype. Individuals with
Rh system
Rh is the most complex of the human blood group systems,
with 45 well-defined antigens. The most immunogenic and
clinically important antigen of the Rh system is D. Between
82% and 88% of Caucasians, about 95% of black Africans
and almost 100% of people from the Far East are D
positive. Anti-D was first discovered by Levine and Stetson
in 1939. It was mistakenly considered identical to an
antibody made by injecting rabbits with rhesus monkey red
cells and was called antirhesus, but it is no longer correct to
use the term rhesus for the D antigen or for the Rh system.
The other main polymorphisms of the Rh system are C/c
and E/e, two pairs of allelic antigens. C has a frequency of
70% and c a frequency of 80% in Europeans. In black
Africans the frequency of c is much higher and the
frequency of C much lower, whereas in eastern Asia the
opposite is the case, with C approaching 100%. In most
populations E has a frequency of about 30% and e about
98%.
Before the 1970s, anti-D was the most common cause of
haemolytic disease of the newborn (HDN). Injection of D-
negative women with anti-D immunoglobulin within 72 h
of giving birth to a D-positive baby prevents the mothers
from producing the anti-D that could damage their
subsequent babies. This prophylactic procedure has made
HDN due to anti-D relatively rare.
The antigens of the Rh system are encoded by two genes,
RHCE and RHD. These genes are highly homologous and
closely linked on chromosome 1. They have very similar
genomic organization, each containing 10 coding exons.
RHCE encodes the C/c and E/e antigens, plus many others
such as Cw, Cx and VS. RHD encodes the many epitopes of
the D antigen. In Caucasians the D-negative phenotype
results from homozygosity for a deletion of RHD. In
Africans about 66% of D negatives have RHD and the
genetic basis for their lack of D antigen is not known. The
products of the Rh genes are polypeptides that are
palmitoylated but, unlike most cell surface proteins, not
glycosylated. The D and CcEe proteins differ by only 32–
35 amino acids, depending on CcEe phenotype. Hydro-
pathy analysis of the amino acid sequences of the Rh
3
 Blood Group Genetics
proteins together with immunological evidence suggests
that the Rh proteins span the red cell surface membrane 12
times, with internal termini and six extracellular loops
(Figure 2).
The D-negative phenotype results from an absence of D
protein in the membrane, explaining the high immuno-
genicity of D compared with other Rh antigens. The C/c
and E/e polymorphisms represent amino acid substitutions
at different positions in the CcEe protein. Rh epitopes are
conformational and may be discontinuous; that is, they are
very dependent on the shape of the whole molecule and
may involve more than one extracellular loop. Conse-
quently, a single amino acid substitution, even within a
membrane-spanning domain, may create a new antigen
and affect the expression of existing antigens. Studies with
monoclonal antibodies have shown that the D antigen
consists of numerous epitopes. There are many variant
phenotypes in which some D epitopes are missing, making
it possible for a D-like antibody to be produced. Some of
these partial D antigens result from missense mutations in
RHD, but most occur because a section of RHD, ranging
from part of an exon to several exons, has been replaced by
the equivalent region of RHCE. These hybrid genes are
probably the product of gene misalignment and intergenic
recombination during meiosis, due either to double
intergenic crossing over or to gene conversion. In addition
to the RHD–CE–D hybrid genes responsible for partial D,
RHCE–D–CE hybrid genes are responsible for some CcEe
variants.
The nonglycosylated Rh proteins are closely associated
in the red cell membrane with a glycoprotein, the Rh-
associated glycoprotein (RhAG), which has sequence and
conformational similarities to the Rh proteins, but has a
single N-glycan (Figure 2). RhAG is encoded by a gene
(RHAG) on chromosome 6. Absence of RhAG from the
red cell membrane due to RHAG-inactivating mutations
prevents expression of the Rh antigens and gives rise to the
rare Rhnull phenotype. Rhnull may also result from
inactivating mutations in RHCE together with deletion
of RHD. The functions of the Rh proteins and RhAG are
not known, but they do resemble membrane transporters
structurally and have sequence homology with a family of
N
RhD or RhCcEe RhAG
Figure 2 Proposed conformation of RhD and RhCcEe proteins, and the N-
glycosylated (N) Rh-associated glycoprotein (RhAG) in the red cell
membrane.
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ammonium transporters. They may also play a role
maintaining the biconcave shape of red blood cells.
Kell system
The Kell system has 23 antigens. K, the original Kell
antigen, has a frequency of about 9% in Caucasians, but
this figure is considerably lower in other races. Anti-K has
the capacity to cause severe HDN and it is recommended
that K-negative girls and women of child-bearing age
should not be transfused with K-positive blood, in order to
prevent the formation of anti-K.
The Kell gene, KEL, encodes a protein that crosses the
membrane once and has a large C-terminal extracellular
domain with six N-glycans and multiple intramolecular
disulfide bonds that ensure that the protein is highly folded.
The Kell polymorphisms represent single amino acid
substitutions within the Kell glycoprotein. The Kell
glycoprotein has sequence homologies with a family of
metalloendopeptidases, but no enzymatic activity has been
detected. Kell glycoprotein appears on early erythroid
progenitors and may play a role in erythropoiesis, although
absence of Kell glycoprotein in the rare Kell-null
phenotype has no pathological effect.
The Kell glycoprotein is linked by a disulfide bond to Kx,
a protein with 10 membrane-spanning domains, encoded
by an X-linked gene, XK. Absence of Kx, due to
inactivating mutations or gene deletion, results in McLeod
syndrome, which is characterized by weakness of Kell
antigens and by varying degrees of acanthocytosis and
muscular and neurological defects.
MNS system
The MNS system, the second blood group system to be
discovered, is now known to be highly complex with 43
antigens and numerous phenotypes. The MNS antigens
are located on one or both of two sialic acid-rich red cell
membrane glycoproteins, glycophorin A (GPA) and
glycophorin B (GPB). These glycoproteins are heavily O-
glycosylated and GPA also has a single N-glycan. The MN
polymorphism represents amino acid substitutions at
positions 1 and 5 of GPA. GPB usually expresses N
because the first 26 amino acids of the most common form
of GPB and the N form of GPA are identical. The Ss
polymorphism represents an amino acid substitution at
position 29 of GPB. GPA and GPB are encoded by
homologous genes, GYPA and GYPB, on chromosome 4.
A third homologous gene, GYPE, may produce a third
glycoprotein, glycophorin E. Like the Rh system, much of
the complexity of the MNS system results from genetic
rearrangements involving GYPA and GYPB and, in at
least one case, GYPE. These rearrangements may involve
unequal crossing over, gene conversion and splice site
mutations, and lead to the formation of hybrid glycophor-

in molecules. In addition there are null phenotypes in
which GPA and/or GPB are absent from the red cells, the
results of gene deletions.
Duffy system
The Duffy polymorphism in people of European and Asian
origin comprises two alleles encoding two antigens, Fya
and Fyb, and three phenotypes, Fy(a 1 b 2 ), Fy(a 1 b 1 ),
and Fy(a 2 b 1 ). In black Africans there is a third allele,
Fy, which produces neither Fya nor Fyb. Homozygosity for
Fy provides a fourth phenotype, Fy(a 2 b 2 ), with a
frequency approaching 100% in west Africa. The Fya/Fyb
polymorphism represents a single amino acid substitution
in the Duffy glycoprotein; the Fy allele has an identical
coding sequence to the Fyb allele, but also has an upstream
nucleotide substitution that disrupts a GATA-1 transcrip-
tion factor binding site and prevents expression of Duffy
glycoprotein in erythroid tissue.
The Duffy glycoprotein, a member of the G protein-
coupled superfamily of receptors, binds proinflammatory
chemokines and is present on red cells and on endothelial
cells lining postcapillary venules throughout the body. In
the Fy(a 2 b 2 ) phenotype, Duffy glycoprotein is absent
from red cells, but is still expressed elsewhere in the body.
Merozoites of the malarial parasite Plasmodium vivax
exploit Duffy glycoprotein as a receptor for attachment
and subsequent invasion. Most African people have no
Duffy glycoprotein on their red cells and are resistant to P.
vivax infection.
Kidd system
Anti-Jka and anti-Jkb of the Kidd system are a hazard in
blood transfusion as they are often difficult to detect yet
can cause severe immediate and delayed haemolytic
transfusion reactions. Jka and Jkb alleles have similar
frequencies in Caucasians, and the frequencies do not differ
greatly in most other populations. The Jka/Jkb polymorph-
ism represents an Asp280Asn substitution in the Kidd
glycoprotein. The Kidd glycoprotein is polytopic, crossing
the membrane 10 times, and has a single N-glycan. It
functions as a urea transporter and is present in endothelial
cells of the vasa recta, the vascular supply of the renal
medulla. The Kidd-null phenotype is extremely rare in
most populations, but has a frequency of about one in 400
in Polynesians. Two Kidd-null individuals were found to
be homozygous for intronic splice site mutations in the JK
gene, responsible for exon skipping and the production of
truncated proteins that did not facilitate urea transport.
Kidd-null red cells have impaired urea transport and,
unlike normal red cells, are not rapidly lysed when
suspended in 2 mol L 2 1 urea. Kidd-null individuals may
have a slight urine concentrating defect, but generally no
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Blood Group Genetics
clinical syndrome has been associated with Kidd-null
phenotype.
Diego system
The 18 antigens of the Diego system represent single amino
acid substitutions within the red cell anion exchanger 1
(AE1) or band 3. AE1 permits the transfer of HCO32 ions
across the red cell membrane in exchange for Cl 2 ions,
rapidly reversing the accumulation of HCO32 in the red
cells and greatly increasing the quantity of carbon dioxide
that the blood can convey to the lungs. AE1 also provides a
link between the plasma membrane and the membrane
skeleton. The Dia/Dib polymorphism represents a Pro854-
Leu substitution; Dia is relatively common in the native
people of the Americas and in China and Japan, but is rare
in people of European and African origin. The Wra/Wrb
polymorphism is associated with a Lys658Glu substitu-
tion, but the high frequency antigen Wrb is not expressed in
the rare phenotypes in which no GPA is present, providing
evidence that AE1 and GPA are associated in the red cell
membrane.
Other systems
The other large blood group system is Lutheran, with 18
antigens. The Lutheran glycoprotein is a member of the
immunoglobulin superfamily (IgSF) of receptors and
adhesion molecules and binds the extracellular matrix
glycoprotein laminin. The LW and Ok glycoproteins also
belong to the IgSF. The Ina/Inb polymorphism of the
Indian system represents a single amino acid substitution
on CD44, a ubiquitous glycoprotein that binds the
extracellular matrix glycoprotein hyaluronan. The Ger-
bich system antigens are on two sialic acid-rich glycopro-
teins, GPC and GPD, encoded by a single gene, GYPC.
Like AE1, GPC and GPD anchor the plasma membrane to
the membrane skeleton. The Cromer and Knops system
antigens are on two complement regulatory glycoproteins,
decay-accelerating factor (CD55) and complement recep-
tor type 1 (CD35), which protect the red cells from attack
by autologous complement. Chido/Rodgers antigens are
on the fourth component of complement, but are not true
blood groups as they become attached to the red cells as
part of a low level or background activation of comple-
ment. The Colton polymorphism represents an amino acid
substitution on a water channel, aquaporin 1 (AQP1).
AQP1, which is strongly expressed in the kidney, plays a
role in reabsorption of water from the renal tubules.
Surprisingly, no pathology is associated with the rare
Colton-null phenotype, in which no AQP1 is produced.
Xga antigen is encoded by an X-linked gene which
straddles the pseudoautosomal boundary on the short
arm of the X-chromosome and escapes X inactivation. The
XG gene is homologous to MIC2, a pseudoautosomal gene
5
 Blood Group Genetics
Table 3 Five platelet surface glycoprotein polymorphisms
Human platelet antigen Alleles Alternative names
A1 A2
HPA-1 a/b Pl /Pl , Zw /Zw
HPA-2 a/b Kob/Koa, Sibb/Siba
HPA-3 a/b Baka/Bakb
HPA-4 a/b Pena/Penb
HPA-5 a/b Brb/Bra
that is active on both X- and Y-chromosomes and encodes
a putative receptor molecule, CD99.
Platelet and Neutrophil Antigens
Since 1959 a number of alloantigenic polymorphisms has
been detected on platelets. Platelet antigens may also be
present on other cells, but are not on red cells. They have
mostly been defined by clinically relevant alloantibodies
that cause posttransfusion purpura (PTP) and neonatal
alloimmune thrombocytopenia purpura (NAITP). In the
numerical terminology for well-defined human platelet
antigens (HPAs), the polymorphisms are numbered, as
opposed to the numbering of genes or gene clusters used in
red cell antigen terminology (Table 3). All these poly-
morphisms represent amino acid substitutions on one of
four platelet glycoproteins. These glycoproteins play
important roles in platelet function, but none of the
polymorphisms has been shown to have any functional
significance. HPA-1 (PlA) and HPA-4 (Pen) antibodies, in
Caucasians and Orientals respectively, are those that are
most commonly responsible for PTP and NAITP.
HPA-1 and HPA-4 polymorphisms are on glycoprotein
GPIIIa (CD61) and several other GPIIIa variants have
been detected. GPIIIa combines with GPIIb (CD41) in the
platelet membrane to form the major platelet integrin,
crucial for platelet adhesion and aggregation. The HPA-3
polymorphisms are on GPIIb. HPA-5 is on the GPIa
(CD49b) subunit of the GPIa–IIa (CD49b/CD29) integrin
that mediates adhesion of platelets to collagen. The GPIb–
V–IX complex of glycoproteins is the major platelet
receptor for von Willebrand factor and is essential in the
adhesion of platelets to vessel walls following vascular
injury. HPA-2 is on the GPIba (CD42ba) component of
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Glycoprotein Polymorphism
a b
GPIIIa (CD61) Leu33Pro
GPIba (CD42ba) Thr145Met
GPIIb (CD41) Ile843Ser
GPIIIa (CD61) Arg143Gln
GPIa (CD49b) Glu505Lys
this complex. Anti-Naka is produced by individuals with
various inactivating mutations resulting in a deficiency of
GPIV (CD36), another platelet collagen receptor.
Antibodies to granulocyte or, more specifically, neu-
trophil antigens (NA) may be responsible for febrile
reactions during blood transfusion, immune neutropenias
and transfusion-related acute lung injury. The NA1/NA2
polymorphism is on FcgRIII (CD16), an immunoglobulin
superfamily glycoprotein that binds aggregated IgG. Other
neutrophil polymorphisms are on CD11a and CD11b, a
subunits of CD11/CD16 integrins, molecules with recep-
tor, adhesion and complement-regulatory functions, and
on other, poorly characterized, glycoproteins.
Class I major histocompatibility complex proteins are
present on red cells, platelets and granulocytes. Because of
the high degee of polymorphism of these ubiquitous
antigens, they are always considered separately from other
blood group antigens.
Further Reading
Anstee DJ and Cartron J-P (1997) Towards an understanding of the red
cell surface. In: Garratty G (ed.) Applications of Molecular Biology to
Blood Transfusion Medicine, pp. 17–49. Bethesda, MD: American
Association of Blood Banks.
Avent ND (1997) Human erythrocyte antigen expression: its molecular
bases. British Journal of Biomedical Sciences 54: 16–37.
Barclay AN, Brown MH, Law SKA et al. (1997) The Leucocyte Antigen
Facts Book, 2nd edn. London: Academic Press.
Daniels G (1995) Human Blood Groups. Oxford: Blackwell Science.
Issitt PD and Anstee DJ (1998) Applied Blood Group Serology, 4th edn.
Durham, NC: Montgomery Scientific Publications.
Mollison PL, Engelfriet CP and Contreras M (1997) Blood Transfusion in
Clinical Medicine, 10th edn. Oxford: Blackwell Science.
Reid ME and Lomas-Francis C (1997) The Blood Group Antigen Facts
Book. London: Academic Press.