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Primate red cell enzymes Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase.

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Primate Red Cell Enzymes: Glucose-6-phosphate
Dehydrogenase and 6-Phosphogluconate
Dehydrogenase
JOHN BUETTNER-JANUSCH,' LAUREN DAME, GEORGE A. MASON
AND DONALD S. SADE
Departments of Anatomy and Zoology, Duke University, Durham,
North Carolina; Caribbean Primate Research Center, Puerto Rico,
a n d Department of Anthropology Northwestern University,
Evanston, Illinois
KEY W O R D S Erythrocyte enzymes
morphism . M a c a c a . Prosimians
.
*
Galago . Genetic polyPropithecus.
ABSTRACT
Glucose-6-phosphate dehydrogenase (E. C . : 1.1.1.49) phenotypes
and 6-phosphogluconate dehydrogenase (E. C . : 1.1.1.44) phenotypes were determined by starch-gel electrophoresis of red cell hemolysates of Galago crassicaud a t u s subspp., Propithecus verreauxi, L e m u r spp., H a p a l e m u r griseus, and
Macaca mulatta. A single glucose-6-phosphate dehydrogenase (G6PD) phenotype
was found in each species. A single 6-phosphogluconate dehydrogenase (6PGD)
phenotype was found in L e m u r spp., H a p a l e m u r griseus, and Galago crassicaud a t u s argentatus. I n a group of six Propithecus verreauxi, three GPGD phenotypes, PGDA, PGDAB, and PGDB, were found. Three phenotypes, PGDA,
PGD AB, and PGD B, were found in 38 G . c. crassicaudatus. The three phenotypes
in each species are apparently the products of two codominant autosomal alleles,
PGDA and PGDE. The frequency of PGD" in G. c. crassicaudatus is 0.263. A population of 260 free-ranging macaques displays a polymorphism a t the GPGD locus.
Three phenotypes, PGD A, PGD AB, and PGD B, were found. These also appear
to be controlled by two codominant autosomal alleles, PGD" and PGD*; the frequency of PGDA = 0.913. Additional analysis of three well-defined troops within
the macaque population indicated that there are no significant differences between the troops or within the population at the GPGD locus.
Variant forms of red cell enzymes are
well known in man, and some examples of
variants of homologous enzymes have
been reported among nonhuman primates
(Schmitt et al.,'70; Barnicot and Cohen,
'70; Tariverdian et al., '71; Kompf et al.,
'71; Barnicot and Hewett-Emmett, '71;
Prychodko et al., '71). In order to increase
our knowledge of these enzymes and their
variants in the Primates, we have examined red cell hemolysates of many species, and we report here some electrophoretic and genetic properties of glucose6-phosphate dehydrogenase (E.C. : 1.1.1.49)
and 6-phosphogluconate dehydrogenase
(E.C.: 1.1.1.44) among seven species of
prosimian primates at the Duke University
Primate Facility (DUPF) and in 260 maAM. J. PHYS. ANTHROP.,41: 7-14.
caques from the Caribbean Primate Research Center at Cay0 Santiago, Puerto
Rico.
Glucose - 6 - phosphate dehydrogenase
(G6PD) and 6-phosphogluconate dehydrogenase (GPGD) are red cell enzymes essential to the sequence of reactions in the
hexosemonophosphate shunt pathway in
aerobic glycolysis (Murphy, '60). The mature red cell, deprived of its nucleus, mitochondria, and Golgi apparatus, can no
longer synthesize proteins or obtain energy
from the Krebs cycle, It can use some of
its remaining enzymes to make some simple compounds. At least 90% of red cell
glycolysis, which provides energy for syn1 Present address: Department of Anthropology, N e w
York University, New York, N.Y. 10003; all correspondence to this address.
7
8
BUETTNER-JANUSCH, DAME, MASON AND SADE
thesis of such compounds, e.g., glutathione,
occurs through the anaerobic pathway,
10% occurs through the aerobic pathway
(Harris, '63). GGPD, in the presence of a
hydrogen ion acceptor, catalyzes the conversion of D-glucose-6-phosphate to Dglucono-&lactone phosphate (6-phosphogluconate). GPGD, also in the presence of
a hydrogen ion acceptor, catalyzes the oxidation of 6-phosphogluconate to D-ribulose-5-phosphate (pentose phosphate) and
C 0 2 ; the pentose phosphate then enters the
Embden-Meyerhof pathway to be converted
to fructose-l,6-diphosphateor glyceraldehyde-3-phosphate.
G6PD occurs in two active forms, tetramers and dimers made up of subunits,
each of which has a molecular weight of
about 50,000 (Cohen and Rosemeyer, '68,
'69; Bonsignore et al., '71a). The interconversion of these two forms in solution
is influenced by pH, ionic strength, and
the presence of M g + + and other divalent
cations (Wrigley et al.,'72; Bonsignore et
al., '71b, '71c). Stability and enzymatic
activity of G6PD are dependent upon the
presence of nicotinamide adenine dinucleotide phosphate (NADP), Removal of NADP
leads to the dissociation of G6PD into inactive monomers (Kirkman et al., '64;
Bonsignore et al., '71a). Electrophoretically
detectable variants have been reported in
human populations, which suggests there
is molecular heterogeneity of G6PD in man
(Porter et al., '64; Kirkman et al., '64;
Dern et al., '66).
The active form of GPGD in man is a
dimer, consisting of identical subunits each
of which has a molecular weight of about
40,000 (Kazazian, '66). Three phenotypes
have been reported in m a n as well as
among several species of macaques (Prychodko et al., '71). After starch-gel electrophoresis, each of the two homozygous human phenotypes (PGD A, the more anodal
on starch gels, and PGD B, the more
cathodal) appears as a single band of
GPGD activity. The two homozygous phenotypes of Macaca mulatta are labeled in
exactly the opposite manner. PGD A is
the more cathodal, PGD B the more anodal (Prychodko et al., '71). I n both man
and macaque, the heterozygous phenotype,
PGD AB, produces three bands of GPGD
activity on starch gels. Two of these are
presumably identical to the bands of activity produced by each of the homozygous
phenotypes; the third band, of intermediate
mobility, is apparently a hybrid molecule
containing a subunit from each allele.
These observations support the view that
two identical subunits form a single GPGD
dimer in homozygotes, each of the dimers
being the product of alleles at the same
locus.
G6PD is inherited as an X-linked trait
in man, and GPGD appears to be inherited
as the product of codominant autosomal
alleles at a single locus.
MATERIALS AND METHODS
Hemolysates were prepared from fresh
blood samples, taken in anticoagulant,
from the following prosimians at DUPF :
64 Galago crassicaudatus subspp., 50
Lemur fulvus subspp., 11 L . catta, 8 L .
macaco, 6 L. variegatus, 6 Propithecus verreauxi coquereli, and 4 Hapalemur griseus.
The macaque hemolysates were obtained
from 260 free-ranging Macaca mulatta living on the island of Cayo Santiago, Puerto
Rico (Altmann, '62; Sade, '67). These 260
animals consist of members of seven distinct troops and 17 peripheral males, or
they were members of troops when the
samples were taken. For three of the troops
currently remaining on the island, troops
labeled F, I, and L, we have sampled almost all of the members.
G6PD and GPGD phenotypes were determined from fresh hemolysates by starchgel electrophoresis in phosphate buffers.
The gel buffer was 0.01 M, pH 7.0; the
buffer i n the electrode trays was 0.1 M,
pH 7.0. Electrophoresis, either vertical or
horizontal, was for 18 hours at 4", 5 volts/
cm.
Because the reactions of G6PD and
6PGD are similar in vitro and because the
methods of staining starch gels are sensitive, we believe it is useful to present some
details of the techniques used in our laboratory for detecting both enzymes. These
techniques are adaptations of those reviewed by Giblett ('69), Motulsky and
Yoshida ('69), and Brewer ('69).
Generally, when we determined only
GGPD, we added 2.5 mg NADP to the
starch before the hot buffer was added and
3.5 mg NADP to the buffer in the cathodal
G6PD AND GPGD OF PRIMATES
electrode tray (Giblett, '69). NADP was
added to demonstrate G6PD if the samples were not run within 72 hours after
they were prepared. We omitted NADP if
the gels were to be used for determining
both G6PD and 6PGD. Gels that contain
NADP have extra cathodal bands on the
half stained for 6PGD; these are nongenetic artifacts. We found no problem
with extraneous bands of GGPD activity if
the gels were run shortly after the samples were drawn, but after electrophoresis
of older samples we generally found nongenetic artifacts. Although GPGD activity
is demonstrable after electrophoresis of
relatively old, properly stored hemolysates,
unambiguous phenotypes cannot always be
determined for such samples, The results
reported here were obtained from samples
no older than 96 hours.
The two enzymes were usually demonstrated on separate halves of the same gel,
and different staining procedures were
used for each enzyme. After the gel was
sliced, strips of excess gel were used to
make a box or fence to enclose the part of
the gel surface to be stained. The boundaries of the box were the origin (site of
insertion of samples), a line about 10 cm
anodal to the origin, and the outer edges
of the gel. The stain for G6PD is made as
follows : 12.0 mg disodium glucose-6-phosphate (G6P), 2.4 mg tetrazolium salts
MTT [ 3- ( 4,5-dimethyl thiazolyl-2 ) -2,5-diphenyl tetrazolium bromide], 2.4 mg
MgCl,.H,O, and 0.5 mg phenazine methosulfate (PMS) are dissolved in 6 ml of a
0.2 M tris-HC1 buffer, pH 8.0. NADP, 2.5
mg, is included if it was omitted from the
gel and electrode buffers. About 10 ml of
warm ( 6 0 " ) 2% melted aqueous agar was
added to the staining solution and this mixture was immediately poured into the box
on the gel surface.
The stain and overlay for GPGD are similar except that 12.0 mg of 6-phosphogluconate (6PG) is used in place of disodium
G6P, and 2.5 m g NADP is added to the
stain whether or not it was in the gel.
The gels with the stain overlay were incubated at 37" for 30 minutes, or until
purple-blue bands appeared, a t which time
the agar overlay was removed. Prolonged
incubation was avoided. Gels that showed
G6PD and 6PGD activity were photo-
9
graphed or sketched shortly after the bands
developed, because the stain is fugitive
and will not remain distinct unless the gels
are kept frozen at about -20". Removing
the agar overlay often lifted part of the
stain from the middle of the colored bands.
Fuzzy smears close to some of the more
distinct bands of 6PGD are, by general
opinion, artifacts that result from the use
of NADP (Giblett, '69).
RESULTS AND DISCUSSION
Except in human control samples, we
found no intraspecific variation of G6PD
after electrophoresis of hemolysates (table 1). The electrophoretic mobility of the
enzyme from Galago crassicaudatus crassicaudatus is indistinguishable from that of
G. c. argentatus; and the enzyme from each
of the subspecies of Lemur fulvus and
from L. macaco has the same electrophoretic mobility. We have no evidence
for or against the hypothesis that G6PD
is X-linked in these nonhuman primates.
Zones of G6PD activity from prosimian
blood samples do not migrate as far anodally as do human controls (fig. 1 j . A
single band that migrates more anodally
than the common human enzyme was
found in samples from all Macaca mulatta
(fig. 1) .
6PGD variants were demonstrated
among Galago crassicaudatus crassicaudatus, Propithecus uerreauxi coquereli,
and Macaca mulatta (tables 1, 2, 3, figs. 1,
2, 3 ) . The patterns on the gels are comparable to those found in human subjects
(Fildes and Parr, '63; Parr, '66; Davidson,
'67) and in several species of macaques
(Prychodko et al., '71 ). Three phenotypes
were found in each of the three species.
In order to avoid a complicated system of
nomenclature and a proliferation of abbreviations for each species, we have simply named the more cathodal bands PGD A
and the more anodal PGD B (Prychodko
et al., '71). It is important to point out
that PGD A of Galago, PGD A of Propithecus, and PGD A of Macaca have different
electrophoretic mobilities; the bands of
PGD B activity for each species are also
different. The distribution of the phenotypes in the three species is shown in tables 2 and 3. In each species the three
phenotypes, PGD A, PGD AB, and PGD 8 ,
10
BUETTNER-JANUSCH, DAME, MASON A N D SADE
TABLE 1
Summary .of observed GGPD and GPGD phenotypes
G6PD
Species
Lorisiformes
Galago crassicaudatus
crassicaudatzts
Galago crassicaudatus
argentatus
Lemuriformes
Lemur f u l v u s subspp.1
L . catta
L. macaco
L. variegatus
Propithecus verreauxi
coquereli
Hapalemur griseus
Cercopithecoidea
Macaca mulatta
Number of
animals
GPGD
Number of
phenotypes
Numberof
animals
Numberof
phenotypes
38
1
38
3
26
1
26
1
50
11
8
6
1
1
1
1
50
11
8
6
1
1
1
1
6
1
1
6
4
4
3
1
260
1
260
3
~________
1
Includes 19 L. f . f u l v u s , 7 L. f. albifrons, 3 L. f . collaris, and 21 L. f . r u f u s .
are probably the products of two codominant, autosomal alleles, PGDA and PGD".
An analysis of pedigrees of Galago crassicaudatus crassicaudatus (Nute e t al., '69)
and Propithecus verreauxi coquereli supports this assumption (table 4 ) . Thus our
data are interpreted exactly as those from
studies of 6PGD in man. Tests of the hypothesis of codominant inheritance of
GPGD activity in our samples of Galago
crassicaudatus crassicaudatus and Macaca
mulatta produced the following xz values,
calculated from estimates of allele frequencies and fit to Hardy-Weinberg expectations: Galago, x; = 0.09, 0.70 < P <
0.80; Macaca, xi = 0.66, 0.30 < P < 0.50.
These tests support the hypothesis.
To our knowledge, this is the first report of a polymorphism at the GPGD locus
in Galago and Propithecus. It should be
noted that the single phenotype found in
Galago crassicaudatus argentatus has the
same pattern as PGD B of G. c. crassicaudatus. The electrophoretic mobilities of
PGD of Lemur spp. and Hapalemur griseus
are identical (fig. 1 ) .
We do not believe it appropriate to subject the data from the DUPF prosimians
to further statistical analysis. The sample
is small, and the animals are highly inbred
(Nute et al., '69). Because of this, we cannot determine whether the founder principle, positive selection, or some other
mechanism is acting at the GPGD locus in
these animals.
The distribution by troop of GPGD
phenotypes of Macaca mulatta and the results of statistical analysis are presented
in tables 3 and 5. For purposes of analysis
we divided the population into four groups :
troop F, troop I, troop L, and all other
troops. The sample of 260 macaques is in
Hardy-Weinberg equilibrium, and each of
the three troops sampled almost in their
entirety, F, I, and L, is also in equilibrium
(table 3 ) . Tests of homogeneity (table 5)
reveal no significant differences between
the macaque troops or within the population of troops.
The frequency of PGD', 0.913, in the
sample of 260 M . mulatta is similar to the
frequency reported by Prychodko et al.
('71) for a sample of 58 animals from
Pakistan, India, and Thailand. These investigators found that continental populations of M . mulatta, as well as continental
populations of M . cyclopis, M . fascicularis
[= M . irus], M . nemestrina, and M . speciosa were polymorphic at the GPGD locus,
Three alleles and five phenotypes were
demonstrated in M . fascicularis [= M .
irus], and two alleles and three phenotypes
in the other species. Island populations
from Taiwan, the Philippines, and Japan
were monomorphic (Prychodko et al., '71).
The polymorphism for the alleles at the
PGD locus in the Cay0 Santiago popula-
11
G6PD AND GPGD OF PRIMATES
GGPD
rinin
6 PGD
+
=
D
t
Origin
1
2
3
4
5
6
7
8
9
1
0
1
1
1
Fig. 1 Relative electrophoretic mobilities of G6PD and 6PGD; conditions of electrophoresis
and methods of staining are given in the text. Bands of G6PD are shown for (1) Lemur
catta, ( 2 ) L. macaco and L. fulvus subspp., ( 3 ) L. variegatus, ( 4 ) Hapalemur griseus, ( 5 )
Propithecus uerrefluxi coquereli, ( 6 ) Galago CTaSSiCaudatus subspp., ( 7 ) Homo sapiens G6PD
A, and ( 8 ) Macaca mulatta. Bands of 6PGD are shown for (1) Galago crassicaudatus crassicaudatus PGD A, ( 2 ) G. c . crassicaudatus PGD AB, ( 3 ) G . c. crassicaudatus and G. c. argentatus PGD B, ( 4 ) Propithecus uerreauxi coquereli PGD A, ( 5 ) P . v . coquereli PGD AB,
( 6 ) P . v . coquereli PGD B, ( 7 ) Macaca mulatta PGD A, ( 8 ) M . mulatta PGD AB, ( 9 ) M.
mulatta PGD B, (10) Lemur spp. and Hapalemur griseus, and (11) Homo sapiens PGD A.
TABLE 2
Distribution of GPGD phenotypes i n Galago and Propithecus
Phenotype
Species
1
2
1
PGDA
PGDAB
PGDB
Total
Galago crassicaudatus
crassicaudatus 2
3
14
21
38
Propithecus uerreauxi
coquereli
3
2
1
6
See text for explanation of nomenclature.
The frequency of PGDA = 0 . 2 6 3 .
12
BUETTNER-JANUSCH, DAME, MASON AND SADE
TABLE 3
Distribution of 6PGD p h e n o t y p e s a n d alleles in Macaca mulatta
Phenotype
Troop
F
I
L
Total
X I
0.80
125
125.00
2.13
10
10.50
1
0.73
49
49.00
0.13
7
6.30
0
0.35
35
35.00
0.43
0
0
0
0
0
0
4
1
12
17
17
51
AB
Obs
EXP
107
105.80
16
18.40
2
Obs
EXP
38
37.77
Obs
EXP
28
28.35
Other
A
E
H
4
J
1
10
16
PM
Total
45
Total
Obs
EXP
1
B
A
PM
1
14
218
216.71
39
41.31
3
1.98
0.920
0.878
0.900
0.941
260
260.00
Frequency
of PGDA
0.913
0.66
peripheral m a l e s .
Fig. 2 Photograph of starch gel stained for 6PGD. The samples are, from left to right,
h u m a n PGD A, Galago crassicaudatus crassicaudatus PGD AB, G . c . crassicaudatus PGD B,
Propithecus verreauxi coquereli PGD B, P. v . coquereli PGD A, P. v . coquereli PGD A; a n d
Macaca mulatta PGD A. The origin is at the bottom, the anode is a t the top; electrophoretic
conditions a n d method of staining a r e described in the text.
13
GGPD A N D GPGD O F PRIMATES
TABLE 4
GPGD genotypes of progeny of irzatings in Galago and Propithecus
Progeny
Matings
PGD '/PGD*
PGDq/PGDn
PGDB/PGDB
Total
0
1
1
0
1
0
2
0
2
4
1
3
4
4
0
2
0
2
Galago crassicaudatus crassicaudatus
PGD"/PGD" X PGDB/PGDB
PGDA/PGDB x PGDA/PGDB
PGDA/PGDB x PGDB/PGDB
PGDB/PGDB x PGDB/PGDB
Propithecus verreauxi coquereli
PGDA/ PGDA x PGDB/PGD3
1
1
Distribution of genotypes
1
1
0
Data from pedigrees of a n i m a l s a t DUPF
variants of malate dehydrogenase occur in
these animals; and albumin and lactate
dehydrogenase are monomorphic (unpublished observations). These data suggest
that we should also consider selection, mutation, and inbreeding as processes contributing to the maintenance of the GPGD
polymorphism. Additional analyses of the
proteins currently being studied in our
laboratory may allow us to specify some
of the reasons for the presence of the polymorphism in this group of macaques.
ACKNOWLEDGMENTS
Fig. 3 Photograph of a portion of a starch gel
stained for GPGD of Macaca mulatta. The samples are, from left to right, PGD A, PGD AB, PGD
A, and PGD A. The origin is at the bottom, the
anode is at the top. Conditions of electrophoresis
and staining are described in the text. The faint
leading band, pronounced in the sample on the
right, occurs only in samples that are more than
48 hours old.
tion is possibly the result of a mixture of
populations; when the Cay0 Santiago population was founded in 1940 it consisted
of groups of macaques imported from several parts of India (Carpenter, '72). The
Cay0 Santiago macaques are also polymorphic at the transferrin locus; rare
We acknowledge with thanks the cooperation and assistance of the staff of the
Caribbean Primate Research Center and
Dr. Jan Bergeron, Managing Director,
Duke University Primate Facility. The work
reported here was supported in part by
National Science Foundation Grant GS
30657X and National Institutes of Health
Grants RR 00388, GM 16722 (Research
Career Development Award to J. B-J.), and
GM 02007 (Training Grant to G.A.M.).
We also acknowledge the assistance of
TABLE 5
T e s t s o f homogeneity of allele
frequencies at the GPGD
locus in macaques
Troops
compared
F/I
F/L
F/ Other
I/L
I/Other
L/Other
Total (x: )
2
x 1
1.52
0.28
0.47
0.21
2.47
1.01
2.89
14
BUETTNER-JANUSCH, DAME, MASON AND SADE
Eastern Airlines personnel who usually delivered blood samples without undue delay.
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phosphogluconate, phosphate, primate, enzymes, red, dehydrogenase, cells, glucose
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