• Title, Summary, Keyword: Udpase

Search Result 3, Processing Time 0.024 seconds

Effects of Chitosan on the Induction of Renal Dipeptidase (RDPase) from the Proximal Tubules (신장의 근위세뇨관에서 Renal Dipeptidase(RDPase)의 유도에 관한 키토산의 효과)

  • Kim, Young-Ho;Yoon, Hyun-Joong;Park, Haeng-Soon;Lee, Myung-Yul;Kim, Jong-Se
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.34 no.7
    • /
    • pp.968-972
    • /
    • 2005
  • The purpose of this study was to evaluate the effects of chitosan, which is deacetylated derivative of chitin, on the renal function. Renal dipeptidase (RDPase, membrane dipeptidase, dehydropeptidase 1, EC 3.4.13.19) is glycosyl phosphatidyl-inositol (GPI)-anchored ectoenzyme of renal proximal tubular microvilli and was related with renal disease including acute renal failure, pyelitis and nephritis. The released RDPase and Udpase activities were assayed by modified fluorometric method. In vitro experimental groups were consisted of group 1, the concentration ranges of 0, 0.01, 0.05 and $0.1\%$ chitosan only, group 2, the concentration ranges of 1, 2 and 4 mM glycerol only, and group 3, the concentration ranges of 0, 0.01, 0.05 and $0.1\%$ chitosan in the presence of glycerol (4 mM). In vivo experimental groups were consisted of group 1 in which rats were treated with glycerol for the purpose of glycerol-induced renal damage, and group 2 in which rats were treated with chitosan plus glycerol. The RDPase release of 0.01, 0.05, and $0.1\%$ chitosan groups were increased in the concentration dependent manner. The RDPase release of 1, 2, and 4mM glycerol groups were decreased in the concentration dependent manner. Chitosan in the presence of glycerol restored the released RDPase activity in the proximal tubules. In vivo, chitosan inhibited the decrease of RDPase release by glycerol in the kidney and blocked the decrease of Udpase activity by glycerol in urine. These results indicated that chitosan was possible as a functional food to control renal function and its diseases.

Two-enzyme coupled fluorometric assay of urinary dipeptidase (이원효소 연쇄반응의 형광분석에 의한 Urinary Dipeptidase의 활성도 측정)

  • Park, Haeng Soon;We, Jeoung Soon
    • Analytical Science and Technology
    • /
    • v.8 no.3
    • /
    • pp.359-364
    • /
    • 1995
  • Urinary dipeptidase(Udpase) was assayed by fluorometric analysis of NADH which was produced from an indicator enzyme, L-alanine dehydrogenase. The reaction mixture was consisted of a dipeptide(L-ala-L-ala), ${\beta}-NAD^+$, L-alanine dehydrogenase in 12.5 mM sodium carbonate buffer, pH 9.0, and urinary dipeptidase which initiated the reaction. The fluorescence intensity of NADH was measured as a function of time with the excitation wavelength at 340nm and emission at 460nm. Comparison of this fluorometric method with the conventional spectrophotometric method utilizing glycyldehydrophenylalanine(Gdp) as substrate provided the correlation coefficient of 0.996 and increased the sensitivity more than ten times.

  • PDF

Effects of Low Temperature during Ripening on Amylose Content and Enzyme Activities Associated with Starch Biosynthesis in Rice Endosperm

  • Baek, Jung-sun;Jeong, Han-Yong;An, Sung-Hyun;Jeong, Jae-Heok;Lee, Hyen-Seok;Yoon, Jong-Tak;Choi, Kyung-Jin;Hwang, Woon-Ha
    • KOREAN JOURNAL OF CROP SCIENCE
    • /
    • v.63 no.2
    • /
    • pp.86-97
    • /
    • 2018
  • The objective of this study was to determine the effects of low temperature on starch accumulation in rice grains. We used four major Japonica-type Korean rice cultivars as materials: Jinbu (JB), Junamjosaeng (JJ), Geumyoung (GY), and Hwawang (HW). Rice plants were moved into two phytotrons the day after heading. Temperatures in the two phytotrons were maintained at $19/29^{\circ}C$ (night/day) as the control, and $13/23^{\circ}C$ as the low temperature condition, both under natural daylight with a relative humidity of 65%. The ripening rates of JB and JJ showed no significant difference between the low temperature and control conditions at 45 days after heading (DAH). In contrast, the ripening rates of GY and HW were 86% and 57% lower than those of JB and JJ under the low temperature condition at 45 DAH, respectively. However, the ripening rates of these four varieties at 61 DAH (when accumulated temperature reached $1,100^{\circ}C$) under the low temperature condition were similar to those at 45 DAH under the control condition (JB, 94%; JJ, 97%; GY, 97%; HW, 88%). The total starch contents showed no significant difference between the control and low temperature conditions. However, the amylose contents in the cultivars were higher under the low temperature than under the control condition. The enzyme activities of starch biosynthesis were about 5-10 days slower in cultivars under the low temperature than under the control. The grain-filling rate showed significant correlations with the enzyme activities of SuSase ($r^2=0.70^{***}$), AGPase ($r^2=0.63^{***}$), UDPase ($r^2=0.36^{***}$), StSase ($r^2=0.51^{***}$), and SBE ($r^2=0.59^{***}$). In conclusion, although StSase activity was increased at $13/23^{\circ}C$ up to 20 DAH, there might not be enough time for SBE to synthesize amylopectin, thus affecting the amylose content of HW, which had the slowest grain filling rate. Notably, the decreased activity of SuSase and SBE and late increase in AGPase activity under the low temperature during the ripening stage are considered to be disadvantageous, as they delay ripening and increase the amylose content.