Molecular features and immunological properties of lactate dehydrogenase C4 isozymes from mouse and rat testes.
With the use of a computer graphics system, spacefilling models of mouse and rat testis lactate dehydrogenase C4 (LDH-C4) isozymes were constructed from amino acid sequence and published x-ray diffraction data. Thirty-two residues that differ between the mouse and rat LDH-C4 sequences are also displayed on the monomeric and tetrameric lactate dehydrogenase molecules. Immunological properties of mouse and rat LDH-C4 isozymes are compared and related to these 32 differences. Possible relationships between the structure, especially the amino acid sequence, and the unique enzymatic properties of LDH-C4 isozymes are also discussed.
D000595:Amino Acid Sequence; D000818:Animals; D000936:Antigen-Antibody Complex; D000939:Epitopes / Q000032:analysis*; D007106:Immune Sera; D005779:Immunodiffusion; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000276:immunology; D008297:Male; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D051381:Rats; D013045:Species Specificity; D013737:Testis / Q000201:enzymology*
D000936:Antigen-Antibody Complex; D000939:Epitopes; D007106:Immune Sera; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase