The common pathogen Salmonella enteirtidis (S. enteritidis) is the major cause of foodborne disease. Protein identification by peptide mass fingerprinting using the matrix-assisted laser desorption ionization time of fight (MALDI-TOF) mass spectrometry (MS) can analysis unambiguously identity the spots from 2-dimensional electrophoresis (2-DE) gel. In this report, we examined protein components from patterns of S. enteritidis proteins. In addition, antigens that are recognized by sera can be identified by immunoblotting.

This study was performed to report the outbreaks of canine intestinal spirochetosis and to characterize the canine isolates. Three canine isolates were weakly beta-hemolytic and had sharp end shape with 5 flagella. Isolates didn't produce indole but fermented fructose. In API-ZYM∨_ study, isolates were alpha-glucosidase negative and alpha-galactosidase positive, which is the typical characteristics of B. pilosicoli. In multilocus enzyme electrophoresis(MEE) study, isolates were divided into 2 electrophoretic types.

The alkaline single-cell gel electrophoresis (SCGE) assay, called the comet assay, has been applied to detect DNA damage induced by a number of chemicals and biological factors in vivo and in vitro. The DNA damage was analysed by tail moment (TM) and tail length (TL), which were markers of DNA strand breaks in SCGE. Human, mouse and rat peripheral blood lymphocytes (PBLs) were irradiated with different doses of ∨60Co γ-rays, e.g. 1, 2, 4, and 8 Gy at a dose rate of 1 Gy/min. A dose-dependent increase in TM (p less than 0.01) and TL (p less than 0.01) was obtained at all the radiation doses (1-8 Gy) in human, mouse and rat PBLs.

Nine strains of Yersinia species isolated from pigs and dogs in Korea, comprising 5 strains of Yersinia enterocolitica, 2 strains of Y. kristensenii and each strain of Y. pseudo-tuberculosis and Y. intermedia, were examined for the presence of virulence-associated plasmids, calcium dependency and provocation of guinea pig conjunctivitis (Sereny test). Three strains of Y. enterocolitica isolated from pigs were positive in calcium dependency and harbored one plasmid of about 45 megadalton, but negative in Sereny test

A total of 466 foremilk from dairy farms in Chonnam Korea [R.] district was examined for the subclinical mastitis over a period of 1 year, using a method of the electrical conductivities (EC); absolute conductivity (AC) and differential conductivity (DC) and quarter difference value (QD), in relation to the California mastitis test (CMT) and the direst somatic cell count (DSCC). The compatibility and efficiency rating between the EC values and the other screening tests was conducted

The activity of lactate dehydrogenase in plasma and various tissues (skeletal muscle, cardiac muscle, liver, lung, kidney and spleen) of Korean native cattle in a Choju abattoir, the Breeding Stock Farm and Animal Farm of Chonbuk University was determined by using ultra violet method. Using polyacrylamide gel electrophoresis, the lactate dehydrogenase isoenzyme distribution of plasma and various tissues in Korean native cattle was studies. The plasma lactate dehydrogenase activity of Korean native cattle was 554.80 +- 92.70 IU/L and the lactate dehydrogenase activity of male plasma was 543.96 +- 97.89 IU/L, which was lower than that of female plasma, 579.19 +- 78.09 IU/L. The plasma lactate dehydrogenase activity of calf was 557.31 +- 110.27 IU/L and was not significantly different from that of adult Korean native cattle. But the range of calf lactate dehydrogenase activity was larger than that of adult Korean native cattle. In tissues, the lactate dehydrogenase activity was decreased in order of lung, kidney, spleen, liver, heart and skeletal muscle. The lung had the greatest activity and the skeletal muscle had the least. Lactate dehydrogenase isoenzymes in plasma and tissues were found to have a characteristic distribution and quantitative isoenzyme patterns. In plasma, the LDH1 usually had the greatest activity and other isoenzymes showed a decreasing tendency in order of LDH2, LDH3, LDH4 and LDH5. The distribution of lactate dehydrogenase isoenzymes had a wide variation in tissues. But the distribution of LDH isoenzymes in plasma was similar to that in kindey, and also cardiac muscle and spleen had similar pattern in LDH isoenzymes distribution