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

IV. Mature RBC
189
TABLE 7.5 Erythrocyte Chemical Constituents of Various Species a
Analyte Cattle Sheep Goat Pig
G6P 52 15 (1) 28 10 (2) 3.2 0.8 (3) 11 (4)
F6P 28 11 (1) 11 2 (2) 1.2 0.7 (3) 4.5 (4)
FDP 16 12 (1) 25 10 (2) 2 (4)
DHAP 35 11 (1) 10 3 (2) 1.0 0.5 (3) 1 (4)
3PG 32 12 (1) 11 21 (2) 53 (4)
2PG 9 4 (1) 14 10 (2) 12 (4)
PEP 19 7 (1) 19 14 (2) 1.0 0.4 (3) 8 (4)
Pyruvate 54 24 (1) 87 21 (2) 22 (4)
Lactate 1989 758 (1) 1623 1203 (2) 14,800 (4)
AMP 40 23 (2) 8 2 (3) 250 (4)
ADP 73 22 (1) 138 31 (2) 17 4 (3) 500 (4)
ATP 633 115 (1) 532 126 (8) 363 52 (3) 1670 (4)
2,3DPG 289 (5) 21 16 (8) 59 28 (3) 9500 (4)
Pi 400 (6) 666 206 (9) 850 (6) 870 (6)
GSH 2490 350 (7) 2257 130 (10) 2500 360 (7)
GSSG 5 (10)
a
Given in nmole/ml RBC, except lactate and pyruvate, which are given in nmole/ml whole blood. Mean values have been recalculated
at times to permit direct comparisons between species. Standard deviation values are given where indicated. Abbreviations: G6P, glucose
6-phosphate; F6P, fructose 6-phosphate; FDP, fructose 1,6-diphosphate; DHAP, dihydroxyacetone phosphate; 3PG, 3-phosphoglycerate;
2PG, 2-phosphoglycerate; PEP, phosphoenolpyruvate; AMP, adenosine monophosphate; ADP, adenosine diphosphate; ATP, adenosine
triphosphate; 2,3-DPG, 2,3-diphosphoglycerate; Pi, inorganic phosphate; GSH, reduced glutathione; GSSG, oxidized glutathione. Figures
in parentheses are the references cited as follows: (1) Zinkl and Kaneko, 1973b; (2) Noble et al. , 1983; (3) Agar and Smith, 1974;
(4) Magnani et al. , 1983; (5) Agar et al. , 1983; (6) Harkness et al. , 1969; (7) Agar et al. , 1974a; (8) Travis et al. , 1985;
(9) Battaglia et al. , 1970; (10) Srivastava and Beutler, 1969.
FIGURE 7-3 Schematic model of the
organization of the RBC membrane
skeleton.
to form tetramers. Multiple spectrin tail ends (an average
of six) are joined together by binding to common short
filaments of actin and a variety of other proteins, including
tropomyosin and adducin, to form an anastomosed
meshwork of polygons ( Fig. 7-4 ). These junctional complexes
with actin are stabilized by other proteins, including
protein 4.1 and protein 55. Protein 4.1 binds the meshwork
to one or more integral membrane glycophorins ( Delaunay,
2007 ). The meshwork is also bound to transmembrane
band 3 by ankyrin in regions of spectrin self-association,
and protein 4.2 may strengthen the ankyrin to band 3 linkage
( Mohandas and Chasis, 1993 ; Rybicki et al. , 1996 ).