Response time of broiler chickens to cimaterol: meat tenderness, muscle composition fiber size, and carcass characteristics.

The response time to cimaterol (CIM), a beta-adrenergic agonist, by broiler chickens for carcass characteristics, muscle composition, muscle fiber size, catheptic enzyme activity, and tenderness was determined. Two trials were conducted in which chickens were fed a control diet (CON) containing 0 ppm of CIM or a diet containing 1 ppm of CIM. Trial 1 consisted of 55, 31-d-old broiler chickens individually fed for up to 48 h. At 0, 6, 12, 18, 24, and 48 h, five CON and five CIM-fed chickens were killed. Trial 2 consisted of 160, 33-d-old broiler chickens group-fed for up to 14 d. At 2, 4, 6, 8, 10, 12, and 14 d, 10 CON and 10 CIM-fed chickens were killed. The breast muscle (BM) and leg muscle (LM) weight, cathepsin B and L activities, DNA, RNA, and protein concentration, and BM shear force value (SFV) were measured in both trials. Thigh muscle (TM) SFV were measured in Trial 2 only. Fiber size of BM was measured (five birds per treatment) at d 2, 6, 10, and 14. In Trial 1, BM weight and SFV were lower in CIM-fed birds at 6 h (P less than .05). In Trial 2 BM SFV were higher at d 8 (P = .06) and d 10 (P less than .05) in CIM-fed chickens. The SFV of CIM-fed chickens were higher at d 4, 8, 10, 12, and 14 (P less than .05).(ABSTRACT TRUNCATED AT 250 WORDS)     

Characterization of Brucella canis protein antigens and polypeptide antibody responses of infected dogs

The cytoplasmic protein antigens (CPAg) of Brucella canis were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and analysis of 35S-labeled polypeptides. Approximate molecular weights of the immunoreactive polypeptides were determined by migration patterns of the immunoprecipitated polypeptides after SDS-PAGE or Western immunoblotting of sera collected at various times after experimental infection of dogs. Polypeptides were specifically precipitated by sera of infected dogs, but not from the sera of normal or false-positive (seropositive, non-infected) animals. During the initial month after infection, proteins with molecular weight masses (MW) of approximately 18, 22, 31, 42 and 54 kDa were commonly recognized. A 20-kDa polypeptide was first recognized at 8-10 weeks after infection, but it was detected inconsistently after 6 months. Additional polypeptides detected from 2 to 12 months post-infection had MW of 22, 66-68 and, less regularly, 42, 60, 82, 100 and greater than 200 kDa. The polypeptides most consistently recognized in sera from B. canis-infected dogs had MW of 18, 22 and 68 kDa.     

An automated micro-method for the enzymatic determination of D-B-hydroxybutyrate in ruminant plasma

1. An enzymatic ‘reaction rate’ micro-method for the rapid routine estimation of D-B-hydroxybutyrate (D-B-HOB) in ruminant plasma, using an I.L. Multistat III centrifugal analyzer, is described.
2. Reaction conditions were optimized to give a linear response for plasma D-B-HOB concentrations between 100 and 2500 μmoles per litre, at 30°C and pH 9.0.
3. For the standardized method the within-run and between-run coefficients of variation for deproteinised ovine plasma were consistently less than 3.5%.
4. There was good agreement between plasma concentrations obtained by the present method and both original U.V. end-point technique (r=0.927b=0.950) and a colorimetric end-point procedure (r=0.937. b=0.879).
5. Utreated ovine and bovine plasma consistently exhibited high ‘blank’ activity and this was directly correlated with plasma lactate dehydrogenase (LDH) activity in both species (r=0.971; p<0.001 and r=0.949; p<0.001 respectively). The distribution of LDH activity in man was similar to sheep but, contrastingly, non-specific interference was extremely low in human plasma and unrelated to LDH. Horse, chicken and rat had negligible ‘blank” activity and comparatively low LDH levels. In both cattle and sheep non-specific interference was abolished by perchloric acid precipitation. In the sheep subtraction of ‘blank’ activity gave D-H-HOB concentrations for untreated plasma comparable to those in deproteinised samples. However, in the bovine, D-B-HOB levels remained significantly (t=6.44; p<0.001) higher even after ‘blank’ correlation. In contrast to man and other non-ruminants, perchloric acid precipitation is essential in ruminants to avoid false overestimation of plasma D-B-HOB levels.
6. Plasma with EDTA as anticoagulant and serum gave concentrations of D-B-HOB approximately 60% lower, than samples containing heparin or oxalate/fluoride. However, heparin was associated with much higher (up to 50%) non-specific NAD rduction than oxalate/fluoride.
7. High levels of acetoacetate (400–1000 μmoles per litre) reduced the recovery of D-B-HOB from ovine plasma by less than 10%. This effect was negated by the inclusion of hydrazine hydrates in the reaction mixture. Perchlorate ion concentrations above 25 μmoles per litre per test dramatically inhibited the assay in ovine plasma, and therefore precipitation conditions must be carefully controlled.
8. Plasma with oxalate/fluoride as anticoagulant showed the greatest stability in storage; 24 hours at room temperature, one week at +4°C and at least one month at ?20°C.