**7. Conclusion**

LDH3

 occurred in low amounts with fairly similar proportions (3–6%). The muscle isoenzyme was also the main fraction in pheasant and turkey serum [8, 27] (44 and 50%, respectively). Heart homotetramer as well as hybrid forms were present in smaller amounts. Most mammals showed a reverse pattern: the main portion of serum lactate dehydrogenase activity

tions (**Figure 1**). The serum pattern of LDH isoenzymes probably reflects the pattern of the main LDH organ donors (heart, skeletal muscle, and liver) and differs from animal to animal species. As an example, the quantitative analysis can serve organ/tissue pattern and relative distribution of LDH isoenzymes in chicken (**Figure 2**) [28]. The patterns of lactate dehydrogenase isoenzymes in various chicken tissues, erythrocytes, and serum can be divided into three groups: (1) those with cathodic domination, (2) those with anodic domination, and (3)

and LDH5

made only minor contribu-

migrated in the first three anodic fractions, while LDH<sup>4</sup>

86 Electrophoresis - Life Sciences Practical Applications

**Figure 2.** Lactate dehydrogenase isoenzymes pattern in chicken tissues and blood.

A suitable method for electrophoretic separation of bird lactate dehydrogenase isoenzymes is isoelectric focusing technique in a pH range of 3–9. It enabled to determine patterns and relative distribution (%) of LDH isoforms in bird sera and tissues (chicken adult and embryonic, as well as turkey). They were characterized by a prevalence of slow moving LDH5 in sera in both species probably originated from breast muscle that distinguish them from mammalian pattern where anodic LDH<sup>1</sup> -LDH3 dominate over cathodic form/s. Mammalian tissues pattern of lactate dehydrogenase isoenzymes differs from species to species with the highest enzyme activity in the skeletal muscle followed by heart and liver. Chicken adult and embryonic lactate dehydrogenases differ each other especially in the pattern of breast muscle with all five isoenzymes being present in the tissue of embryonic origin.

[5] Dawson DM, Goodfriend TL, Kaplan NO. Lactic dehydrogenases: Function of the two

Lactate Dehydrogenase Isoenzyme Electrophoretic Pattern in Serum and Tissues of Mammalian…

http://dx.doi.org/10.5772/intechopen.76322

89

[6] Fondy TP, Kaplan NO. Structural and functional properties of the H and M subunits of lactic dehydrogenases. Annals of the New York Academy of Sciences. 1965;**119**:888-903 [7] Heinová D, Blahovec J. Lactate dehydrogenase isoenzymes in mammalian and fowl sera

[8] Heinová D, Blahovec J, Rosival I. Lactate dehydrogenase isoenzyme pattern in bird, carp and mammalian sera. European Journal of Clinical Chemistry and Clinical Biochemistry.

[9] Cahn RD, Kaplan NO, Levine L, Zwilling E. Nature and development of lactic dehydrogenases. The two major types of this enzyme form molecular hybrids which change in

[10] Wilson AC, Cahn RD, Kaplan NO. Functions of the two forms of lactic dehydrogenase

[11] Roussel JD, Stallcup OT. Distribution of lactic dehydrogenase and transaminase in the genital tissues of Holstein-Friesian bulls. Journal of Dairy Science. 1967;**50**:1306-1309

[13] Wu KC, Chan K, Lee CY, Lau YF. Molecular isolation and sequence determination of the cDNA for the mouse sperm-specific lactate dehydrogenase—X gene. Biochemical and

[14] Li SSL, Fitch WM, Pan YCE, Sharief FS. Evolutionary relationship of vertebrate lactate dehydrogenase genes A (muscle), B (heart) and C (testis). Journal of Biological

[15] Quattro JM, Woods HA, Powers DA. Sequence analysis of teleost retina specific lactate dehydrogenase C: Evolutionary implications for the vertebrate lactate dehydrogenase gene family. Proceedings of the National Academy of Sciences of the United States of

[16] Goldberg E, Eddy EM, Duan C, Odet F. LDHC the ultimate testis specific gene. Journal

[17] Zinkham WH, Isensee H. Genetic control of lactate dehydrogenase synthesis in the somatic and gametic tissues of pigeon. Johns Hopkins Medical Journal. 1972;**130**:11-25

[18] Salehi-Ashtiani K, Goldberg E. Differences in regulation of testis specific lactate dehydrogenase in rat and mouse occur at multiple levels. Molecular Reproduction and

[19] Tsoi SCM, Li SSL. The nucleotide and deduced amino-acid sequences of a cDNA encoding lactate dehydrogenase from *Caenorhabditis elegans*: The evolutionary relationship of lactate dehydrogenases from mammals, birds, amphibian, fish, nematode,

[12] Holmes RS. Evolution of lactate dehydrogenase genes. FEBS Letters. 1972;**28**:51-55

types. Science. 1964;**143**:929-933

1996;**34**:91-95

(in Slovak). Veterinary Medicine—Czech. 1994;**39**:75-84

makeup during development. Science. 1962;**136**:962-969

in the breast muscle of birds. Nature. 1963;**197**:331-334

Biophysical Research Communications. 1987;**146**:964-970

of Andrology. 2010;**31**:86-94. DOI: 10.2164/jandrol.109.008367

Chemistry. 1983;**258**:7029-7032

America. 1993;**90**:242-246

Development. 1993;**35**:1-7
