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고착협 내탈립 기계수확 적응 장류⋅두부용 콩 품종 ‘새금’
김현태(Hyun Tae Kim),한원영(Won Young Han),이병원(Byung Won Lee),고종민(Jong Min Ko),이영훈(Yeong Hoon Lee),백인열(In Youl Baek),윤홍태(Hong Tai Yun),하태정(Tae Joung Ha),최만수(Man Soo Choi),강범규(Beom Kyu Kang),김현영(Hyun Yeong K 한국육종학회 2019 한국육종학회지 Vol.51 No.4
The soybean cultivar, ‘Saegeum’, has been developed for preparing soy-paste and tofu. The soybean cultivars ‘Daepung’ and ‘SS98207-3SSD-168’ were crossed in 2003 to obtain ‘Saegeum’. Single seed descent method was used to advance the generation from F3 to F5, and the plant lines with promising traits were selected from F6 to F7 by pedigree method. The preliminary yield (PYT) and advanced yield trials (AYT) were conducted from 2009 to 2010, and the regional yield trial (RYT) was conducted in 12 regions between 2011 and 2013. The morphological characteristics of ‘Saegeum’ were as follows: determinate plant type, white flower, tawny pubescence color, and brown pod color. Flowering and maturity dates were August 2, XXXX and October 17, XXXX, respectively. Plant height, first pod height, number of nodes, number of branches, and number of pods were 79 cm, 18 cm, 16, 2.3, and 44, respectively. The seed characteristics of ‘Saegeum’ were as follows: yellow spherical shape, yellow hilum, and the 100-seed weight was 25.4 g. ‘Saegeum’ was resistant to bacterial pustule and SMV in the field test, and its lodging resistance was mildly strong, whereas its shattering resistance was excellent. The ability of this cultivar to be processed into tofu, soybean malt, and other fermented products was comparable with that of ‘Daewonkong’. The yield of ‘Saegeum’ in the adaptable regions was 3.02 ton ha-1. Thus, ‘Saegeum’ is adaptable to mechanized harvesting because of its high first pod height, as well as lodging and shattering resistance. (Registration number: 5929)
Thioacetamide에 의한 BALB/c 마우스 간의 시간별 약물대사효소 억제 양상 : A Time-Course Study
이정운,고우석,김갑호,배연경,하현정,한상섭,천영진,정태천 영남대학교 약품개발연구소 2001 영남대학교 약품개발연구소 연구업적집 Vol.11 No.-
Thioacetamide is a potent hepatotoxicant which requires metabolic activation by cytochrome P450s (P450s) for toxicity. In the present study, the elevation kinetic of serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) activities by thioacetamide treatment was investigated in male BALB/c mice. Inaddition, the inhibitory effects of thioacetamide on liver microsomal P450 enzymes were further investigated. Thioacetamide at 100 mg/kg/ was treated intraperitoneally for 6, 12, 24, 36, 48 and 72 hr. The blood was collected at the designated time for assaying the serum enzyme activities. To determine the P450 isozyme-specific activities. ethoxyresorufin O-deethylase (EROD), methoxyresorufin O-demethylase (MROD), and benzyloxyresorufin O-debenzylase (BROD) activities were determined for P450 1A1, 1A2 and 2B1, respectively, in liver microsomal fractions. The activities of ALT and AST were started to be elevated 6 hr after thioacetamide treatment andreached the maximun at 36 hr after the treatment. The elevated activities were dramatically recovered at 72 hr. The microscopic exmination of the liver specimen also showed a similar profile of hepatotoxicity. All P450-associated enzyme activities were time-dependently inhibited by the treatiment with thioacetamide. The maximum inhibition of P450 enzymes was observed 36 hr after the treatment. Because the inhibition of P450 enzymes by thioacetamide was time-dependent, our present results suggest that thioacetamide might inhibit P450 enzymes in mechanism-based inactivation.
Oxidation of Rosmarinic Acid Catalyzed by Mushroom Tyrosinase
Tae Joung Ha,Myoung-Hee Lee,Hyun Sook Kwon,Byeong Won Lee,Chang-Hwan Park,Suk-Bok Pae,Chan-Sik Jung,Keum-Yong Park 한국응용생명화학회 2011 Applied Biological Chemistry (Appl Biol Chem) Vol.54 No.4
Rosmarinic acid isolated from the Perilla frutescens (L.) was found to possess mushroom tyrosinase (EC 1.14.18.1) inhibitory activities with an IC50 of 4.0 μM. However, rosmarinic acid was oxidized as a substrate catalyzed by tyrosinase. The oxidation kinetics of mushroom tyrosinase by rosmarinic acid measured by spectrophotometic and polarographic methods showed Km=166.8 μM, 225.1 μM and Vmax=16.26 μM/min, 3.05 mg O2/L/min, respectively.
Slow-Binding Inhibition of Soybean Lipoxygenase-1 by Luteolin
Tae-Joung Ha,장대식,Myoung-Hee Lee,Hyun-Tae Kim,Hyun Sook Kwon,In-Youl Baek,Isao Kubo 대한약학회 2012 Archives of Pharmacal Research Vol.35 No.10
Luteolin, isolated from the seeds of Perilla frutescens (perilla seeds), inhibited the peroxidation of linoleic acid catalyzed by soybean lipoxygenase-1 (EC 1.13.11.12, Type 1) with an IC50 of 5.0 μM (1.43 μg/mL)noncompetitively. The progress curves for an enzyme reaction indicate that luteolin shows slow binding kinetics. Both the initial velocity and steady-state rate in the progress curve were decreased with increasing the concentration of luteolin. The kinetic parameters, which described the inhibition by luteolin, were evaluated by nonlinear regression fits.
Ha, Tae-Joung,Lee, Jin-Hwan,Hwang, Seon-Woo,Lee, Jun,Kang, Nam-Suk,Park, Keum-Yong,Suh, Duck-Yong,Park, Ki-Hun,Yang, Min-Suk The Korean Society for Applied Biological Chemistr 2006 Journal of Applied Biological Chemistry (J. Appl. Vol.49 No.1
The flowers of Hemisteptia lyrata B. afforded two known acylglycerylgalactosides, 2',3'-di-O-(9Z,12Z,15Z-octadecatrienoyl)glyceryl ${\beta}$-D-galactopyranoside (1) and 2'-O-(9Z,12Z,15Z-octadecatrienoyl)glyceryl ${\beta}$-D-galactopyranoside (2), and a new sesquiterpene galactopyranoside, 7-eudesmene-1${\beta}$,4${\beta}$-diol-1-O-${\beta}$-D-galactopyranoside (3). This is the first time that galactopyranosides (1-3) have been isolated from the genus Hemisteptia. Their structures and stereochemistry were elucidated by 1D and 2D NMR data, including COSY, NOESY and HMBC experiments.
Oxidation of Rosmarinic Acid Catalyzed by Mushroom Tyrosinase
Ha, Tae-Joung,Lee, Myoung-Hee,Kwon, Hyun-Sook,Lee, Byeong-Won,Park, Chang-Hwan,Pae, Suk-Bok,Jung, Chan-Sik,Park, Keum-Yong The Korean Society for Applied Biological Chemistr 2011 Applied Biological Chemistry (Appl Biol Chem) Vol.54 No.4
Rosmarinic acid isolated from the Perilla frutescens (L.) was found to possess mushroom tyrosinase (EC 1.14.18.1) inhibitory activities with an $IC_{50}$ of $4.0{\mu}M$. However, rosmarinic acid was oxidized as a substrate catalyzed by tyrosinase. The oxidation kinetics of mushroom tyrosinase by rosmarinic acid measured by spectrophotometic and polarographic methods showed $K_m=166.8{\mu}M$, $225.1{\mu}M$ and $V_{max}=16.26{\mu}M$/min, 3.05 mg $O_2$/L/min, respectively.