Effects of evisceration and storage temperature on changes in meat quality of traditional farm‐fresh Turkeys

1. Conditions affecting the keeping quality of traditional farm‐fresh turkeys were investigated.

2. Storage of uneviscerated Wrolstad turkeys at 4 °C for 10 days caused no statistically significant changes in meat flavour or texture.

3. During further storage at —2 °C, however, there was a slight but significant change in flavour, which became more marked with time in birds which had been eviscerated after the initial period at 4 °C.

4. Both eviscerated and uneviscerated birds became slightly tougher during storage.

5. Initial holding at 4 °C increased the numbers of psychrotrophic bacteria on the skin by about 10³ but subsequent changes at — 2 °C were slight for uneviscerated birds.

6. Eviscerated carcases had higher counts than uneviscerated birds after storage at — 2 °C and, although ‘off’ odours were not detected, spoilage appeared to be imminent at the end of the 20‐d period.     

Effect of age and sex on the eviscerated yield,muscle and edible offal of a commercial broiler strain

1. Comparisons of the effects of age (up to 364 d) and sex on the rate of growth, eviscerated yield, blood loss and yield of skin, breast, thigh and drumstick muscles, heart, liver and gizzard have been made on a commercial British broiler strain.

2. Male broilers grew linearly up to 76 d whereas the females grew more slowly after 35 d. At 364 d the difference in live body weight was small.

3. Up to 56 d, males had a slightly higher eviscerated yield. There was no significant difference between the sexes beyond this age.

4. The proportional yield of breast muscle was variable with age, whereas that of thigh and drumstick increased with age in the male, particularly at 175 and 364 d.

5. After 35 d the proportion of skin was larger in females, whereas the gizzard as a proportion of live body weight in both sexes decreased rapidly between 21 and 76 d. Blood loss during killing was always higher in male broilers after 21 d.     

Skin blackening during the cooking of spent laying fowls

1. Blackening of the skin in factory processed cooked hens has been associated with elevated copper levels.

2. The degree of blackening was not directly related to copper content although the latter level was always higher than in control hens.

3. Simulated factory procedures, using scald water at 53 °C or 60 °C containing 50 mg Cu²⁺/1 and 50 mg C1₂/1, produced blackened skins of varying intensity on cooking.

4. It is suggested that the problem arose from a malfunction of the chlorination plant which produced excessive levels of chlorine and low pH, followed by erosion of copper from water pipes and subsequent interaction of copper and chlorine with the chicken skin.     

Experimental infection of normal and immunosuppressed pigs with Pseudomonas pseudomallei

A single dose of 5 x 10(8) bacilli of Pseudomonas pseudomallei by intratracheal injection resulted in acute (21 cases) or chronic (19 cases) melioidosis in 40 of 48 pigs. Fifteen (10 acute and 5 chronic) had been immunosuppressed by cyclophosphamide before inoculation. The major clinical signs were initial fever, marked neutrophilia and, in the acute cases, respiratory distress. There were no signs of the nasal and ocular discharge, paresis or diarrhoea seen in acute cases in south-east Asia. The cyclophosphamide treatment caused a significant decrease in the neutrophil count by 7 d after inoculation in all 15 immunosuppressed pigs, and all were culture positive at necropsy. Eight of the 33 non-treated pigs were culture negative at necropsy. Pigs overcoming the initial phase of infection had more abscess-like nodules that were bacteriologically sterile at necropsy than the pigs with acute cases of melioidosis. P. pseudomallei was isolated predominantly from the spleen, lungs and the injection site. Although only one strain was used in this study, it is likely that Australian strains of P. pseudomallei are not as virulent as the south-east Asian isolates.     

Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors

Phospholipase C gamma 1 (PLC gamma 1) and p21ras guanosine triphosphatase (GTPase) activating protein (GAP) bind to and are phosphorylated by activated growth factor receptors. Both PLC gamma 1 and GAP contain two adjacent copies of the noncatalytic Src homology 2 (SH2) domain. The SH2 domains of PLC gamma 1 synthesized individually in bacteria formed high affinity complexes with the epidermal growth factor (EGF)- or platelet derived growth factor (PDGF)-receptors in cell lysates, and bound synergistically to activated receptors when expressed together as one bacterial protein. In vitro complex formation was dependent on prior growth factor stimulation and was competed by intracellular PLC gamma 1. Similar results were obtained for binding of GAP SH2 domains to the PDGF-receptor. The isolated SH2 domains of other signaling proteins, such as p60src and Crk, also bound activated PDGF-receptors in vitro. SH2 domains, therefore, provide a common mechanism by which enzymatically diverse regulatory proteins can physically associate with the same activated receptors and thereby couple growth factor stimulation to intracellular signal transduction pathways.     

The relation between major histocompatibility complex (MHC) restriction and the capacity of Ia to bind immunogenic peptides

The capacity of purified I-Ad, I-Ed, I-Ak, and I-Ek to bind to protein derived peptides that have been previously reported to be T cell immunogens has been examined. For each of the 12 peptides studied strong binding to the relevant Ia restriction element was observed. All the peptides bound more than one Ia molecule; however, for 11 of 12 peptides, the dominant binding was to the restriction element, whereas in one instance the dominant binding was to a nonrestriction element. When the peptides were used to inhibit the presentation of antigen by prefixed accessory cells to T cells, an excellent correlation was found between the capacity of a peptide to inhibit the binding of an antigen to purified Ia and the capacity of the peptide to inhibit accessory cell presentation of the antigen. Thus, the binding of peptide to purified Ia is immunologically relevant, and Ia seems to be the only saturable molecule on the surface of the accessory cell involved in antigen presentation. Inhibition analysis also indicated that all peptides restricted to a particular Ia molecule competitively inhibited one another, suggesting that each Ia restriction element has a single binding site for antigen. Cross-linking of labeled peptides to Ia followed by electrophoretic analysis and autoradiography suggested that this single binding site is made up of portions of both alpha and beta chains of Ia.