Effects of the hunting method on meat quality from fallow deer and wild boar and preliminary studies for predicting lipid oxidation using visible reflectance spectra

This study examines the influence of hunting methods on the colour and lipid oxidation state of meat from wild boar (Sus scrofa) and fallow deer (Dama dama). In addition, the feasibility of using visible reflectance spectra (360 to 740 nm) to predict the lipid oxidation of meat was evaluated. A total of 25 wild boars and 14 fallow deer were hunted with two different methods, dog-driven hunting (DH) and harvest culling (HC), that imply different animal stresses before shooting. Lipid oxidation increased in the meat from both species, which had been frozen for 3 months. The increase was higher in the DH group than the HC group (P?<?0.05). Our results confirm the importance of hunting stress on meat quality and lipid stability. The multivariate regression analysis showed a high correlation (R ²?=?0.968) between the predicted and measured thiobarbituric acid-reactive substances (TBARS) values, suggesting that visible spectroscopy should prove useful for predicting meat oxidation.     

Comparison of Mycoplasma agalactiae isolates by pulsed field gel electrophoresis, SDS-PAGE and immunoblotting

Abstract We have analyzed 81 isolates of Mycoplasma agalactiae from four different regions of Italy between 1990 and 1995 in order to identify antigenic differences through SDS-PAGE and Western blotting and chromosomal DNA restriction endonuclease cleavage pattern differences. Antigenic variability in M. agalactiae isolates was investigated analyzing hydrophobic membrane protein fractions by immunoblotting using pooled sheep antiserum from naturally infected sheep. Large restriction fragments obtained cleaving genomic DNAs with Sma I, Nru I, Sal I, Xho I, Bss HII and Kpn I were analyzed by pulsed field gel electrophoresis. Genetic analysis indicates that isolates are all similar without intraspecific differences. This homogeneity was confirmed by immunoblotting: 80 and 50 kDa antigens are present in all strains analyzed.     

Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymes

Sulphydryl groups of mitochondrial aspartate aminotransferase from horse heart were titrated with 5,5'-dithiobis (2-nitrobenzoic acid). From analysis of peptic peptides, 378 amino acid residues (94.3% of the total) in the protein were identified. The results of amino acid sequence analysis are compared with those of cytosolic and mitochondrial aspartate aminotransferases from other sources.