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Ontogeny of epinephrine, norepinephrine, dopamine-beta-hydroxylase, and chromogranin A in the adrenal gland of pigs.
1996
Laroche S.M. | Pinxteren J.A. | Reempts P.J. van | Potter W.P. de | Weyns A.A. | Verhofstad A.A. | Acker K.J. van
Amino acid profiles in dogs with chronic renal failure fed two diets.
1992
Hansen B. | DiBartola S.P. | Chew D.J. | Brownie C. | Berrie H.K.
Amino acid profiles and serum albumin and serum total protein concentrations were evaluated in dogs with renal disease. Nine dogs ranging in age from 1 to 15 years were identified as having mild to moderate chronic renal failure (CRF; exogenous creatinine clearance, 0.5 to 2.13 ml/kg of body weight/min). These dogs and a group of 10 clinically normal control dogs were fed a diet containing 31% protein for 8 weeks, at which time serum and urine amino acid assays and clearance studies were performed. All dogs then were fed a diet containing 16% protein for 8 weeks and then reevaluated. Chronic renal failure was associated with mild abnormalities in serum concentrations of amino acids. When fed the higher protein diet, dogs with CRF had lower serum concentrations of glutamine, leucine, proline, and serine and higher serum concentrations of cystathionine and 3-methylhistidine than clinically normal control dogs. When fed the low protein diet, dogs with CRF had lower serum serine concentrations and higher serum concentrations of cystathionine, phenylalanine, and 3-methylhistidine. Urine excretion of amino acids in all dogs on both diets was low, and dogs with CRF had lower renal clearances of 3-methylhistidine than control dogs. There were no significant differences in concentrations of serum albumin and total solids between either group, regardless of diet. We concluded that dogs with mild to moderately severe CRF have mild abnormalities of serum free amino acid concentrations, but renal conservation of essential amino acids is not impaired.
Mostrar más [+] Menos [-]Diagnostic implications of detection of proteinase K-resistant protein in spleen, lymph nodes, and brain of sheep.
1992
Race R. | Ernst D. | Jenny A. | Taylor W. | Sutton D. | Caughey B.
Brain, spleen, and selected lymph nodes from sheep with clinical signs of scrapie were analyzed for presence of proteinase K-resistant protein (PrP-res). Diagnosis of scrapie on the basis of detection of PrP-res was compared with diagnosis on the basis of histologic evaluation of the brain from clinically affected or exposed sheep. Proteinase K-resistant protein was found in every brain that was histologically positive for scrapie, and in addition, was found in the brain of several clinically positive sheep that were not diagnosed as scrapie-positive by histologic evaluation. Proteinase K-resistant protein was also found in 87% of the spleens and lymph nodes from sheep that had PrP-res detected in brain homogenates. Therefore, analysis of sheep brain, spleen, or lymph nodes for PrP-res provided a diagnostic approach that was superior to histologic examination alone for detection of naturally scrapie agent-infected sheep.
Mostrar más [+] Menos [-]Effect of dietary protein on functional, morphologic, and histologic changes of the kidney during compensatory renal growth in dogs.
1991
White J.V. | Finco D.R. | Crowell W.A. | Brown S.A. | Hirakawa D.A.
Two diets similar in caloric density and mineral content, but markedly different in protein content, were used to study the effects of dietary protein on renal function and morphologic and histopathologic changes in dogs that had functional renal tissue reduced by seven-eighths nephrectomy. The effects of moderate protein intake (MPrI = 15% protein; dry-matter basis) and high-protein intake (HPrI = 31% protein; dry-matter basis) were studied for the initial 7 months (period 1 [P1]) after renal mass reduction. Diets were then switched between groups during the following 7 months (period 2 [P2]) to evaluate the effects of increased or decreased protein intake. The HPrI caused significantly (P < 0.05) greater glomerular filtration rate (GFR) and renal growth than did MPrI during P1. Dogs that maintained HPrI during P1 and MPrI during P2 (group 1) had significant (P < 0.05) reduction in GFR during P2. Dogs that maintained MPrI during P1 and HPrI during P2 (group 2) had significant (P < 0.05) improvement in GFR and renal growth during P2. At the end of the study, renal reserve was evaluated in both groups of dogs before and after group 1 was returned to HPrI for 2 weeks. During this 2-week feeding trial, group-1 dogs had marked improvement in renal reserve, relative to group 2, and GFR increased to the terminal P1 values. Results indicate a possible residual benefit from HPrI during the early phase of compensatory renal growth in the form of functional compensatory memory to HPrI. The severity of renal lesions was indistinguishable between dogs of dietary groups during both study phases. Plasma electrolyte concentrations rapidly returned to normal range after renal ablation, but mild azotemia and proteinuria persisted throughout most of the study. High protein intake was not associated with increased degree or progression of proteinuria.
Mostrar más [+] Menos [-]Isoelectric focusing under dissociating conditions for analysis of muscle protein from clinically normal dogs and Labrador Retrievers with hereditary myopathy.
1989
Mehta J.R. | Braund K.G. | McKerrell R.E. | Toivio Kinnucan M.
Protein profiles of whole homogenates of anconeus (slow twitch) and biceps femoris (fast twitch) muscles of clinically normal dogs and of Labrador Retrievers with hereditary myopathy (HM) were resolved on flat bed polyacrylamide isoelectric-focusing gels. Three methods of sample solubilization were performed. The solubilization buffer, with high concentrations of urea, precipitated the zwitterionic detergent, but use of the buffer containing 3% NP-40, 9.2M urea, and 0.1M arginine resulted in better resolution and stability of pH gradient. Gels of anconeus muscle from clinically normal dogs contained 2 protein bands specific to anconeus muscle, whereas gels of biceps femoris muscle from clinically normal dogs contained 3 protein bands amplified in biceps femoris muscle that were barely detectable in anconeus muscle. The staining intensity of protein bands in biceps femoris muscles from Labrador Retrievers with HM was decreased, relative to controls. The quantitative analysis of peak height ratios of biceps femoris muscle revealed significant (P less than 0.05) differences between profiles of clinically normal dogs and Labrador Retrievers with HM.
Mostrar más [+] Menos [-]Proteins specified by bovine herpesvirus-2.
1988
Adams S.W. | Balachandran N. | Hutt Fletcher L.M.
Viral and viral protein specificity of antibodies induced in cows persistently infected with noncytopathic bovine viral diarrhea virus after vaccination with cytopathic bovine viral diarrhea virus.
1988
Bolin S.R.
Neutralizing and nonneutralizing antibodies to bovine viral diarrhea (BVD) virus were detected in 3 cows persistently infected with noncytopathic BVD virus after vaccination with modified-live cytopathic BVD virus. Neutralizing antibodies detected in serum samples from each persistently infected cow at 3 weeks after vaccination were highly specific for certain isolates of cytopathic BVD virus and reacted only with a viral protein with a molecular weight of 53,000. Neutralizing antibodies to 1 of 3 isolates of noncytopathic BVD virus were detected in a serum sample obtained at 12 weeks after vaccination from 1 of 3 persistently infected cows. Nonneutralizing antibodies were detected in all cows at 7 to 12 weeks after vaccination.The nonneutralizing antibodies were less specific for isolates of BVD virus and reacted with viral proteins with molecular weights of 115,000, 80,000, 53,000, and 47,000.
Mostrar más [+] Menos [-]Lactate dehydrogenase isoenzymes in blood and cerebrospinal fluid from healthy Beagles.
1986
Heavner J.E. | Colaianne J. | Roper M.
Partial purification and characterization of eosinophil chemotactiv factors from soluble extract of Fasciola species.
1986
Horii Y. | Fujita K. | Owhashi M.
Characterization of Tritrichomonas foetus antigens, using bovine antiserum.
1986
Hall M.R. | Huang J.C. | Ota R. | Redelman D. | Hanks D. | Taylor R.E.L.