Introduction: In calves, hyposelenosis degenerates skeletal muscles in different parts of the body. The extent of damage to muscle cells can be diagnosed by determining the activity of creatine kinase (CK), aspartate aminotransferase (AST), and lactate dehydrogenase (LDH). The aim of this study was to analyse variations in the serum levels of LDH isoenzymes in calves with nutritional muscular dystrophy (NMD), to determine the applicability of this parameter for diagnosing NMD, and to describe the influence of hyposelenosis on total protein (TP), triglyceride (TG), and cholesterol (CHOL) levels.

To differentiate the origin of high total lactate dehydrogenase (LD) activity in canine sera, a spectrophotometric method based on the preferential inhibition of cardiac LD isoenzymes by pyruvate was performed. Comparison with the electrophoretic separation of LD isoenzyme activities and determination of the hydroxybutyrate dehydrogenase-to-LD ratio indicated that the method proposed gave a better discrimination between cardiac and hepatic LD activities than did the other tests.

isoenzyme patterns of extracts of adult schistosomes collected from Hippopotamus amphibius in Kruger National Park compared with similar extracts of adult Schistosoma mansoni and S. rodhaini, characteristics differed suggesting that H. amphibius schistosome is separate species

High serum alkaline phosphatase (ALP) activity is considered a sensitive marker of cholestasis in most mammalian species, including dogs. Induction of high serum ALP activity in association with cholestasis is dependent on high hepatic bile acids concentrations. Treatment of dogs with glucocorticoids also results in high serum ALP activity. The possible causal relation between serum ALP activity and bile acids concentration was investigated in dogs treated with glucocorticoids. The relation of glucocorticoid treatment to changes in the activity of individual ALP isoenzymes, alanine transaminase (ALT) and gamma-glutamyltransferase (GGT) also was investigated. Eight conditioned dogs were given 4 mg of prednisone/kg of body weight, IM, daily for 10 days. Blood samples were taken prior to treatment and on treatment days 3, 5, 7, and 10. Liver tissue was then taken from each dog. Serum total ALP activity was significantly (P < 0.05) high at day 3 in prednisone-treated dogs. Isoenzyme analysis indicated that this increase was attributable to an increase in the liver ALP isoenzyme (LALP). Significant increases in serum corticosteroid-induced ALP (CALP) and bone ALP were first observed on days 7 and 10, respectively. Serum ALT and GGT activities were significantly increased by day 5. Increased serum or hepatic tissue bile acids concentrations were not observed in prednisone-treated dogs, compared with values in 8 clinically normal (control) dogs, but were high in 3 dogs with complete bile duct ligation. Hepatic activities of LALP, CALP, and GGT were higher in prednisone-treated dogs than values in controls, indicating probable increased hepatic synthesis of these enzymes. Hepatic ALT activity was not increased. The ratio of serum to tissue LALP activity was increased in prednisone-treated dogs, compared with values in controls, indicating that LALP may have been preferentially released into serum. There was no difference in the ratio of serum to liver GGT activity between prednisone-treated dogs and controls. The LALP and GGT ratios were increased in bile duct-obstruction dogs. It was concluded that, although LALP is the principal ALP isoenzyme in serum during the first 10 days of prednisone treatment, hepatic bile acid concentrations are not increased and, therefore, are not likely to be responsible for induction and release of ALP into serum. Prednisone may, therefore, be directly responsible for induction of ALP activity in dogs treated thusly.

Corticosteroid-induced alkaline phosphatase (CALP) and intestinal alkaline phosphatase (IALP) from dogs were purified to homogeneity, as determined by polyacrylamide gel electrophoresis. Purification involved an uninterrupted system using DEAE-cellulose, concanavalin A-agarose, and monoclonal antibody affinity columns. The monoclonal antibody was prepared by use of IALP as the antigen. The 2 isoenzymes were compared, using molecular weight determinations, amino acid analyses, peptide mapping, N-terminal sequencing of the first 10 amino acids, carbohydrate analyses, and recognition by anti-IALP monoclonal antibody. The data indicated that canine IALP and CALP are identical with regard to recognition by monoclonal antibody and N-terminal amino acid sequence, nearly identical in amino acid content and peptide maps, but different in carbohydrate content. It was concluded that CALP is a product of the same gene as IALP and that differences in glycosyl transferase activities between liver and intestines or the presence of glycosidase activities in or around the intestinal mucosae result in the marked difference in carbohydrate content.

This paper reviews the alkaline phosphatases in canine serum, the analytical methods used for qualitative and/or quantitative detection of these isoenzymes, and the diagnostic significancy of each of these isoenzymes. The paper further describes some of the latest advances of our knowledge of the canine alkaline phosphatases and possible areas of future research