Clinical Biochemistry of Domestic Animals (Sixth Edition) - UMK ...

IV. Mature RBC
187
TABLE 7-3 Erythrocyte Enzymes of Various Animal Species a
Enzyme Cattle Sheep Goat Pig
HK 0.36 0.14 (1) 0.58 0.07 (3) 0.52 0.15 (4) 0.18 0.12 (5)
GPI 17.0 1.0 (1) 19.8 2.6 (3) 79.1 8.5 (4) 90.9 16.3 (5)
PFK 2.43 1.26 (1) 1.53 0.14 (3) 2.33 0.46 (4) 1.23 0.85 (5)
Aldolase 1.46 (2) 1.28 0.13 (3) 1.44 0.71 (4) 0.78 0.67 (5)
TPI 300 17 (3) 589 122 (4) 719 211 (5)
GAPD 43.3 (2) 57.2 5.2 (3) 73.7 10.2 (4) 40.6 (5)
PGK 16.2 7.3 (1) 49.6 2.6 (3) 87.8 18.3 (4) 94.2 63.7 (5)
MPGM 10.0 4.5 (1) 18.7 1.5 (3) 19.3 6.7 (4) 27.3 12.6 (5)
Enolase 3.15 0.98 (1) 8.15 0.51 (3) 13.9 2.0 (4) 8.58 6.45 (5)
PK 5.72 1.13 (1) 2.82 0.22 (3) 5.00 1.23 (4) 12.5 4.8 (5)
LDH 23 (2) 33.6 3.5 (3) 17.5 3.05 (4) 28.7 5.9 (5)
DPGM 0.42 (6) 0.04 (6) 0.58 (6)
DPGP 0.03 (6) 0.01 (6) 0.01 (6)
G6PD 5.40 0.49 (1) 0.76 0.13 (3) 2.06 0.46 (4) 17.3 1.2 (5)
6PGD 0.84 0.19 (1) 0.58 0.24 (4) 3.3 1.4 (5)
GR 0.69 0.47 (7) 2.60 0.22 (3) 3.87 1.57 (4) 2.6 0.8 (7)
GPx 165 (8) 164 21 (3) 179 55 (4)
GST 4.7 0.5 (9) 7.8 1.0 (9) 8.0 (13) 1.4 0.2 (9)
SOD 2060 75 (10) 1910 100 (10) 1240 100 (10)
Catalase ( 10 3 ) 81 (8) 16.6 1.5 (12)
Cb 5 R 1.83 0.24 (1) 2.00 0.12 (3)
Na , K -ATPase nil (11) HK
, 3 1 (11)
LK , nil 10 2 (11)
a
All enzyme units are U/g Hb, except ATPase given in μ moles phosphorus liberated/g Hb/h. Mean values have been recalculated at times to permit direct
comparisons between species. Standard deviation values are given where indicated. Abbreviations: HK, hexokinase; GPI, glucose phosphate isomerase;
PFK, phosphofructokinase; TPI, triosephosphate isomerase; GAPD, glyceraldehyde-3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; MPGM,
monophosphoglycerate mutase; PK, pyruvate kinase; LDH, lactate dehydrogenase; AST, aspartate aminotransferase; DPGM, diphosphoglycerate mutase;
DPGP, diphosphoglycerate phosphatase; G6PD, glucose-6-phosphate dehydrogenase; 6PGD, 6-phosphogluconate dehydrogenase; FAD, fl avin adenine
dinucleotide; GR, glutathione reductase; GPx, glutathione peroxidase; GST, glutathione S-transferase; SOD, superoxide dismutase; Cb 5 R, cytochrome-b 5
reductase; Na -K -ATPase, Na -K -adenosine triphosphatase. Temperatures above 25°C are included in reference citations. Figures in parentheses are the
references cited as follows: (1) Zinkl and Kaneko, 1973b; (2) Smith et al. , 1972b; (3) Agar and Smith, 1973; (4) Agar and Smith, 1974; (5) McManus,
1967; (6) Harkness et al. , 1969; (7) Agar et al. , 1974a; (8) Kurata et al. , 1993; (9) Del Boccio et al. , 1986; (10) Maral et al. , 1977; (11) Gupta
et al. , 1974 (at 44°C); (12) Suzuki and Agar, 1983; (13) Board and Agar, 1983.
most of the phosphatidylethanolamine) located in the inner
layer or leaflet of the bilaminar membrane. After uptake
from plasma, these phospholipids are shuttled (flipped) from
the outer leaflet to the inner leaflet by an ATP-dependent
aminophospholipid-specific translocase or flippase ( Zwaal
et al. , 1993 ). Most of the cationic choline-containing phospholipids,
phosphatidylcholine (lecithin) and sphingomyelin,
are located in the outer layer ( Delaunay, 2007 ). These
choline-containing phospholipids are readily exchangeable
with plasma phospholipids, whereas the aminophospholipids
are not ( Reed, 1968 ). RBCs also contain a Ca 2 -dependent
phospholipid scramblase that is activated by a protein kinase
C catalyzed phosphorylation. This scramblase accelerates
the bidirectional transbilayer movement of phospholipids.
The inhibition of the flippase or the activation of the scramblase
can result in increased phosphatidylserine in the outer
layer, which promotes coagulation and erythrophagocytosis
( Delaunay, 2007 ; Mandal et al. , 2005 ).
Species vary in RBC membrane phospholipid compositions
( Garnier et al. , 1984 ; Nelson, 1967 ; Wessels and
Veerkamp, 1973 ). Cattle, sheep, and goat RBCs are unique in
that their membranes contain little or no phosphatidylcholine