• KOREAN JOURNAL OF CROP SCIENCE
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• v.56 no.1
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• pp.23-28
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• 2011

Resveratrol has been associated with reduced cardiovascular disease and reduced cancer risk. This phytochemical has been reported in a number of plant species including grapes, peanuts and pine trees in response to stress such as fungal infection, heavy metal ions or UV irradiation. The objective of this study was to determine the resveratrol contents in leaves of mulberry varieties at different collecting times. Quantitative analysis of 16 cultivars showed a range of $102{\sim}466{\mu}g/100g$ on dry weight basis (which is equivalent to $25{\sim}116.5{\mu}g/100g$ on fresh weight basis). Resveratrol contents in mulberry leaves was higher in autumn than spring, and higher in fully matured leaves than in juvenile leaves. Among the tested samples, 'Kaeryangppong', 'Sugeppong' and 'Cheongilppong' collected in the middle of October showed high resveratrol contents of $838{\mu}g/100g$, $803{\mu}g/100g$, $800{\mu}g/100g$ on dry weight basis, respectively. Especially mulberry leaves dried in the shade showed of $1,030{\mu}g/100g$ on dry weight basis in resveratrol content, this result may contribute to utilization of mulberry leaves.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.24 no.5
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• pp.273-288
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• 1991

To elucidate the physiological and biochemical differences between chondrichthyes and osteichthyes, the properties of the specific digestive enzymes in cat-shark, Cephaloscyllium umbratile, and mackerel, Scomber japonicus, were studied. Homogenous trypsin proved through the disc-electrophoresis, SDS-PAG electrophoresis and gel filtration was obtained from the pancreas of cat-shark by $50-70\%$ saturated ammonium sulphate fractionation, DEAE-Sephadex A-50 column chromatography, benzamidine-Sepharose 6B affinity chromatography and Sephadex G-75-120 gel filtration. Two types of trypsins were also obtained from the pyloric caeca of mackerel by $30-70\%$ saturated ammonium sulphate fractionation and the slightly modified procedure from the method adopted in the purification of cat-shark trypsin. The two trypsins, designated trypsin A and B, were proved their homogeneity by disc- and SDS-PAG electrophoresis and gel filtration. The molecular weights of the trypsins were estimated to be 31,700 for cat-shark trypsin, 30,000 for mackerel trypsin A and 29,000 for mackerel trypsin B by SDS-PAG electrophoresis, but those were estimated to be 21,500 for cat-shark trypsin, 23,700 for mackerel trypsin A and 21,500 for mackerel trypsin B by gel filtration. The trypsins exhibited their optimum conditions at pH 9.0 and on temperature ranged from $45^{\circ}C\;to\;50^{\circ}C$ for cat-shark, and at pH 8.0 and a temperature of $50^{\circ}C$ for mackerel trypsin A and B, respectively. The cat-shark trypsin was stable at pH 10.0 and the temperature below $10^{\circ}C$, whereas the mackerel trypsin A and B, were stable in the range over pH 7.0 to pH 9.0 below $10^{\circ}C$ and at pH 8.0 below $35^{\circ}C$, respectively. The mackerel trypsins were severely inhibited by some heavy metal ions such as $Ag^{2+},\;Cu^{2+}\;and\;Hg^{2+}$ compared to cat-shark trypsin. All of the enzymes were also inhibited by antipain, leupeptin, TLCK(tosyllysine chloromethyl ketone) and SBTI(soybean trypsin inhibitor) remarkably. The inhibitory effects of PMSF(phenylmethane sulphonylfluoride), DFP(diisopropyl fluorophosphate) and benzamidine were indicated that these enzymes belong to serine-proteases.