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오덕철,김선균,주왕기,조동현,김우호,윤경민 江原大學校附設體力硏究所 1976 江原大學校附設體育科學硏究所論文集 Vol.- No.1
The water quality of the Hong-Cheon river was investigated during the winter season. The rate of contamination of the low tide was a little more than the high tide. But all values of the analyzed-items were similar to those in the clear water.
Physicochemical Properties of Heme Iron Products in the Korean Market
Uh-Hyun Kim,Young-Mi Shin,Mie-Jae Im,Seon-Yong Kim 한국식품영양과학회 2006 Journal of medicinal food Vol.9 No.2
Since absorption efficacy of heme iron (HI) is critically dependent on its solubility in aqueous solution, we in-vestigated the physicochemical properties of two HI products available in the Korean market. The two HI products did notdiffer in ingredients and color. However, HI polypeptide (HIP), produced in Korea, was fairly soluble over a wide pH rangein water-based solutions, whereas HI imported from Japan was insoluble except in strong acid and base solutions. Analysisusing an ultraviolet-visible spectrophotometer showed that the chromophore of HIP was shifted to the red compared with thatof HI. Fourier transform-infrared analysis revealed that HIP contained mainly amide (NH) groups, while HI largely containedamine (NH2) groups. With regard to constituents, between HIP and HI, their major components were different from each otheraccording to their ratio of fronts obtained by thin-layer chromatography. These results suggest that determination of solubil-ity should be included in the quality control process of HI products.
Properties of Poly ( ADP - ribose ) Sythetase from the Sprout of Glycin Max Linne ( Soybean )
Kim, Uh Hyun,Won, Jong Jin,Kim, Hyung Rho 생화학분자생물학회 1986 BMB Reports Vol.12 No.4
The effect of pH, mono-and divalent canons, sodium dodecyl sulfate, N-ethylmaleimide, ouabain, sodium azide and several steroid hormones on Ca^(2+)-ATPase activity of sarcoplasmic reticulum isolated from conger eel (Astroconger myriaster) muscle were examined. The results obtained were as follows: 1. Ca^(2+)-ATPase of conger eel muscle sarcoplasmic reticulum showed its maximum activity at pH 7.4. 2. Monovalent cations used in this study increased Ca^(2+)-ATPase activity. The order of effectiveness of monovalent canons tested at 100mM concentration in increasing the activity of ATPase is K^+ $gt; Na^+ $gt; Li^+ $gt; NH₄^+, Ca^(2+)-ATPase activity was inhibited by divalent cations with the following order of effectiveness at 0.5 mM concentration: Cd^(2+) $gt; Co^(2+) $gt; Sr^(2+) $gt; Mn^(2+) $gt; Zn^(2+) 3. Ca^(2+)-ATPase activity was inhibited significantly by sodium dodecyl sulfate and N-ethylmaleimide but not affected by ouabain and sodium azide. 4. Ca^(2+)-ATPase activity was slightly inhibited by 17α-hydroxypregnenolone and β-estradiol, and severely inhibited by hydrocortisone at all concentrations used in this study. 5. β-pregnan-3β-ol-20-one, dehydroisoandrosterone and corticosterone activated Cat+-ATPase activity slightly at low concentrations and at high concentrations, 5α-pregnan-3β-ol-20-one did not exert any influence on ATPase activity but dehydroisoandrosterone and corticosterone inhibited enzyme activity severely.
A New Assay Method for Ornithine Aminotransferase
Kim, Uh Hyun,Kim, Hyung Rho,Lee, Gye Jeong,Park, Jin Woo 생화학분자생물학회 1986 BMB Reports Vol.13 No.4
An attempt was made to develop a new assay method for ornithine aminotransferase which catalyze the transfer of δ-amino group of ornithine to α-ketoglutamate-γ-semialdehyde and glutamate. Glutamate-γ-semialdehyde(or pyrroline-5'-carboxylic acid), one of the reaction products was found to produce a colored compound showing a peak absorbance at 510 ㎚ with ninhydrin in hot acidic solution, whereas ornithine and glutamate production and color intensity indicated that the enzyme activity could be properly assayed by reading the change of absorbance at 510 ㎚. The enzyme activity measured by new assay method was widely distributed in mouse tissues, especially high in small intestine, kidney and liver, and was mainly present in cytoplasmic fraction of small intestine and in mitochondrial fraction of liver. The enzyme activity showed increasing tendency in liver and kidney with age, in contrast to decreasing tendency in small intestine. The enzyme from hepatic mitochondrial fraction had nearly identical properties to that from intestinal cytoplasmic fraction, such as heat stability in the presence of pyridoxal phosphate, pH activity curves, Km values, for ornithine and α-ketoglutarate, suggesting that they are rather an identical-enzyme than isoenzymes.