Search Results

You are looking at 1 - 3 of 3 items for :

  • Author or Editor: Walter E. Hoffmann x
  • Clinical Pathology x
  • Refine by Access: All Content x
Clear All Modify Search

SUMMARY

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 Aagarose, 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.

Free access
in American Journal of Veterinary Research

Summary

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 γ-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 prednisonetreated 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.

Free access
in American Journal of Veterinary Research

SUMMARY

Assay procedures for determining serum haptoglobin concentration and ceruloplasmin oxidase activity in dogs were validated, and reference values were established. Serum haptoglobin concentration is reported as milligrams per deciliter of cyanmethemoglobin binding capacity, whereas serum ceruloplasmin oxidase activity was determined by use of p-phenylenediamine as substrate. Both assays were used to analyze serum samples from 288 dogs. In each dog’s case record, clinical history and final diagnosis were evaluated to determine whether the dog had an inflammatory condition. Complete blood cell counts were performed in 265 dogs, using simultaneously collected blood samples. Plasma fibrinogen concentration was determined for 161 dogs. A positive correlation (P < 0.01) was found for serum haptoglobin concentration and for ceruloplasmin oxidase activity, compared with wbc counts, segmented neutrophil and band neutrophil counts, and plasma fibrinogen concentration. Ceruloplasmin oxidase activity and haptoglobin concentration were up to 6 times more sensitive than fibrinogen concentration or leukocyte counts in detecting inflammation. Specificity of ceruloplasmin oxidase activity was comparable to fibrinogen concentration and leukocyte counts, whereas haptoglobin concentration was found to be slightly less specific. Specificity of haptoglobin concentration improved slightly (from 0.82 to 0.88) when dogs with a history of glucocorticoid administration were excluded from analysis. Predictive value of a negative test result (haptoglobin concentration < 125 mg/dl; ceruloplasmin oxidase activity < 20 IU/L) and predictive value of a positive test result for haptoglobin concentration and ceruloplasmin activity were comparable to or better than fibrinogen concentration or various oxidase leukocyte counts in detection of inflammation in a variety of disease conditions. We concluded that serum haptoglobin and ceruloplasmin oxidase assays could be used as adjuncts for diagnosis of the inflammation in dogs.

Free access
in American Journal of Veterinary Research