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

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186<br />

Chapter | 7 The Erythrocyte: Physiology, Metabolism, and Biochemical Disorders<br />

TABLE 7-2 Erythrocyte Enzymes <strong>of</strong> Various Animal Species a<br />

Enzyme Human Dog Cat Horse<br />

HK 1.78 0.38 (1) 0.92 0.47 (2) 2.01 0.35 (2) 1.45 0.22 (2)<br />

GPI 24.1 1.0 (3) 16.3 1.8 (3) 49.0 8.3 (3) 27.3 5.9 (3)<br />

PFK 11.0 2.3 (1) 9.7 1.3 (2) 2.2 0.7 (2) 8.7 2.5 (2)<br />

Aldolase 3.19 0.86 (1) 2.36 0.32 (4) 2.71 0.98 (9)<br />

TPI 2111 397 (1) 436 70 (4)<br />

GAPD 226 42 (1) 54.4 2.8 (4) 59.0 (6) 57.2 14.2 (9)<br />

PGK 320 36 (1) 89.6 9.4 (4) 29.2 (6) 69.1 19.8 (9)<br />

MPGM 37.7 5.6 (1) 4.04 1.19 (4) 6.35 (6) 5.7 (6)<br />

Enolase 5.39 0.83 (1) 0.84 0.16 (4) 13.6 3.9 (9)<br />

PK 15.0 2.0 (1) 8.4 2.0 (2) 24.5 7.2 (2) 1.7 0.8 (2)<br />

LDH 200 26 (1) 52.2 5.0 (4) 15.1 2.2 (8) 32.3 3.6 (9)<br />

AST 3.02 0.67 (1) 3.14 1.10 (2) 1.53 0.27 (7)<br />

DPGM 2.00 (6) 1.02 (6) 0.08 (6) 0.6 (6)<br />

DPGP 0.021 (6) 0.010 (6) 0.005 (6) 0.006 (6)<br />

G6PD 8.3 1.6 (1) 11.3 2.0 (2) 15.3 3.2 (2) 18.6 3.3 (2)<br />

6PGD 8.78 0.78 (1) 6.73 1.30 (2) 6.88 1.11 (2) 2.61 0.68 (2)<br />

GR ( FAD) 7.18 1.09 (1) 3.60 0.96 (2) 9.31 2.31 2.69 0.99 (2)<br />

GR ( FAD) 10.40 1.50 (1) 5.59 1.05 (2) 20.31 2.21 4.28 1.31 (2)<br />

GPx 31 5 (1) 213 82 (2) 330 54 (2) 149 62 (2)<br />

GST 6.7 1.8 (1) 3.2 0.9 (2) 35.6 8.5 (2) 6.4 1.7 (2)<br />

SOD 2352 (5) 2118 (5) 2885 (5)<br />

Catalase (10 3 ) 153 24 (1) 10 2 (2) 161 43 (2) 105 21 (2)<br />

Cb 5 R 19.2 3.8 (1) 11.3 1.6 (2) 9.8 2.1 (2) 13.0 3.0 (2)<br />

NADPH-D 0.51 0.12 (3) 0.33 0.06 (3) 0.39 0.06 (3) 0.70 0.06 (3)<br />

Na , K -ATPase 8 2 (10) nil (10) nil (10) 5 2 (10)<br />

a<br />

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<br />

comparisons between species. Standard deviation values are given where indicated. Abbreviations: HK, hexokinase; GPI, glucose phosphate isomerase;<br />

PFK, phosph<strong>of</strong>ructokinase; TPI, triosephosphate isomerase; GAPD, glyceraldehyde-3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; MPGM,<br />

monophosphoglycerate mutase; PK, pyruvate kinase; LDH, lactate dehydrogenase; AST, aspartate aminotransferase; DPGM, diphosphoglycerate mutase;<br />

DPGP, diphosphoglycerate phosphatase; G6PD, glucose-6-phosphate dehydrogenase; 6PGD, 6-phosphogluconate dehydrogenase; FAD, fl avin adenine<br />

dinucleotide; GR ( FAD), glutathione reductase with FAD added to assay; GR (FAD), glutathione reductase without FAD added to assay; GPx, glutathione<br />

peroxidase; GST, glutathione S-transferase; SOD, superoxide dismutase; Cb 5 R, cytochrome-b 5 reductase; NADPH-D, reduced nicotinamide adenine<br />

dinucleotide phosphate diaphorase; Na -K -ATPase, Na -K -adenosine triphosphatase. Temperatures above 25°C are included in reference citations. Figures<br />

in parentheses are the references cited as follows: (1) Beutler, 1984 (at 37°C, except Cb 5 R at 30°C); (2) Harvey et al. , unpublished, 2007 (at 37°C, except<br />

Cb 5 R at 30°C); (3) Harvey and Kaneko, 1975a; (4) Maede and Inaba, 1987 (at 37°C); (5) Kurata et al. , 1993; (6) Harkness et al. , 1969; (7) Franken<br />

and Schotman, 1977; (8) Schechter et al. , 1973; (9) Smith et al. , 1972a; (10) Gupta et al. , 1974 (at 44°C).<br />

names. Electrophoretic patterns <strong>of</strong> membrane proteins on<br />

SDS-PAGE are species variable ( Gillis and Anastassiadis,<br />

1985 ; Kobylka et al. , 1972 ; Smith et al. , 1983a ; Whitfield<br />

et al. , 1983 ).<br />

1 . Lipids<br />

The lipid bilayer and associated transmembrane proteins<br />

chemically isolate and regulate the cell interior. The bilayer<br />

consists <strong>of</strong> phospholipids arranged with hydrophobic hydrocarbon<br />

chains <strong>of</strong> fatty acids to the center <strong>of</strong> the bilayer and<br />

the polar ends <strong>of</strong> the molecules in contact with both intracellular<br />

and extracellular aqueous environments. Molecules<br />

<strong>of</strong> unesterified cholesterol are intercalated between fatty<br />

acid chains in molar concentrations approximately equal<br />

to the sum <strong>of</strong> the molar concentrations <strong>of</strong> phospholipids.<br />

Phospholipids are asymmetrically arranged, with anionic<br />

amino-containing phospholipids (phosphatidylserine and

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