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복령 ( Poria cocos ( Schw . ) Wolf ) 중의 Carboxyl Proteinase 의 분리정제 및 그 성질에 관한 연구 ( 1 )
민태진,정광식,김재웅 ( Tae Jin Min,Kwang Sik Chung,Jae Woong Kim ) 생화학분자생물학회 1983 BMB Reports Vol.16 No.3
The enzymic properties of carboxyl proteinase isolated from the Poria cacos (Schw.) Wolf. were investigated. Two kinds of active fraction I and II were isolated from this mushroom. The active fraction II showed carboxyl proteinase activity to bovine hemoglobin substrate, and its optimum conditions were the followings: temperature, 70℃, pH stability, 1.2∼2.5 and thermal stability, 20°∼75 ℃. The enzyme appeared to be one subunit, and consisted of 18 kinds of amino acids. The apparent molecular weight were 25,500 (PAGE) and 23,000(HPLC), respectively. The enzyme appeared to hydrolyze peptide bond between glutaml-L-tyrosine. The Km value of this enzyme was 0.29 mM when carbobenzoxy-L-tyrosine were used as a subtrate.
누에(Bombyx mori L)에 요소 및 Eleutherococcus Senticosus Maxim 첨식효과에 관한 연구
민태진,Min, Tae-Jin 생화학분자생물학회 1982 한국생화학회지 Vol.15 No.2
누에에 요소 1,600 ppm(U) 및 가시오가피 메탄올 추출물 1,200 ppm(E) 수용액을 각각 뽕잎에 처리하여 첨식시켰다. Cellulose acetate(CA) 및 disc-polyacrylamide gel(PAG) 전기영동으로 5령기말 암컷누에의 체내단백질의 영통상의 변화 그리고 가스-크로 마토그라파에 의하여 체내지방산의 함량변화를 대조군(C)과 비교하였다. CA전기영동은 C군 및 U군에 서는 albumin이 주 pattern이었으나 E군은 ${\alpha}$-globulin이었다. disc-PAG 전기영동 결과 C군와 E군은 동일하였으나 U군의 pattern III은 a,b 두개로 분리되었다. Sephadex G-150으로 크로마토그라피한 첫째번 분획들을 disc-PAG 전기영동한 결과 다같이 2째번 pattern이 urease이었다. 또한 3째번 분획들을 정제하여 SDS-PAG 전기영동에 의한 걷보기 분자량은 다같이 46,000 및 26,000이었으나, U군에서 57,000인pattern 1개를 더 관찰하였다. 체내지방산은 6종류로, 미리스트산, 팔미트산, 스테아르산, 올레산, 리놀레산 및 리놀렌산 이었으나 C군에 비하여 E군 U군 순으로 크게 증가하였다. Two groups of the silkworms feeding on mulberry leaves treated with solution of 1,600 ppm of urea (U) and 1,200 ppm of methanol extract of Eleutherococcus senticosus maxim (E), respectively, in comparison with control group (C) were observed. On the end of the fifth instar stage of the female silkworm, significant differences were observed in the body fluid's protein patterns and contents of fatty acid of treatment groups compared with control group. The main patterns of CA-electrophoresis in the C group and U group were albumin and ${\alpha}$-globulin in the E group. Pattern III by disc-polyacrylamide gel (PAG) electrophoresis was double patterns in the U group and a single pattern in C and E group. In the three groups, second pattern by disc-PAG electrophoresis of the first division from Sephadex G-150 gel fractionation was urease. The apparent molecular weights in the purified third division by SDS-PAG electrophoresis were, in the three groups, 46,000 and 26,000. However, another pattern with 57,000 was observed in the U group. Fatty acids in silkworms by gas-chromatography contents myristic acid, palmitic acid, stearic acid, oleic acid, linoleic acid and linolenic acid. Their content were; the greatest in the U group followed by E group and C group.
누에 ( Bombyx mori L . ) 의 요소첨식 효과에 관한 연구
민태진,김택영 ( Tae Jin Min,Taik Yung Kim ) 생화학분자생물학회 1978 BMB Reports Vol.11 No.3
The change of the growth rate, the weight of cocoon, and the change of Urease activity, nucleic acid, protein contents, and the changes in disc electrophoretic patterns of the protein in the silkworm (Suwon No 108×107 confused species) from the 3rd instar stage to the 5th instar stage by supplemental feeding of different concentrations of Urea has been studied. On the experiment group, U₄ which was treated with 1,600ppm Urea, the rate of growth increased to 17. 43% and the rate of cocoon`s weight increased 20.11% more than the control groups. The activity of Urease was increased with the increasing of the concentration of Urea treatment, but not more than the control groups. Beyond U₄ activity of Urease was decreased gradually with the increasing of the concentration of Urea. The contents of nucleic acid were decreased sharply at first in the Urea treatments but gradually increased according to the Urea concentration. In the 5th instar stage, disc electrophoretic patterns of protein in. the silkworms were found to be five in the U₄ group compared to six in the control group.
흰느타리버섯 ( Pleurotsu cornucopiae ( pers ) Rolland ) 중의 Protease 의 분리정제 및 그 성질에 관한 연구 ( 1 )
민태진,홍성일,김재웅 ( Tae Jin Min,Sung Il Hong,Jae Woong Kim ) 생화학분자생물학회 1983 BMB Reports Vol.16 No.1
The enzyme properties of protease of the Pleurotus Cornucopiae (Pers.) Rolland were investigated by purification with gel filteration using DEAE-sephadex A-50, CM-cellulose, DEAE-cellulose and Sephadex G-75. Two kinds of active fractions were isolated from this mushroom study. The active fraction showed protease activity for the bovine serum albumin substrate, and its optimum pH, optimum temperature, pH stability and thermal stability were 4.0, 50℃, 3.0∼4.0 and 20∼40℃, respectively. The activity of the enzyme was inhibited by Ca^(++), Cu^(++), Zn^(++), Fe^(++) and Mg^(++), but increased with Co^(++). The enzyme had one subunits composed of 17 amino acids. The apparent molecular weight was about 56,000 daltons.
흰느타리버섯 ( Pleurotus cornucopiae ( Per . ) Rolland ) 중의 Protease 의 분리정제 및 성질에 관한 연구 ( 2 )
민태진,이수용,김재웅 ( Tae Jin Min,Soo Young Lee,Jae Woong Kim ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.2
The enzymic properties of protease in the Pleurotus cornucopiae(Per.) Rolland were investigated. The Km value was 0.45 mM when hippuryl-L-phenylalanine was used as a substrate. This enzyme showed substrate specificity hydrolyzing the peptide bond of glycyl-L-phenylalanine. This enzyme was inhibited by L-lysine, diazoacetyl-DL-norleucine methyl ester(DAN), 1,2-epoxy-(p-nitrophenoxy)propane(EPNP) and EDTA, also was inhibited by anion as SO₃^(-2), SO₄^(-2) and HP₄^(-2) but increased with NO₂^(-2) ion. The L-cysteine was found to be competitive inhibitor and its K_i value was determined to be 2.4 mM by Dixon plot.
민태진,박혜련,배강규 ( Tae Jin Min,Hye Lyoun Park,Kang Gyu Bae ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.4
The activities of purified ATPase in L. edodes were inhibited by 1-fluoro-2,4-dinitrobenzene (FDNB), N,N`-dicyclohexylcarbodiimide(DCCD), ethacrynic acid(EA) and carbonylcyanide mchlorophenylhydrazone(CCCP), but were stimulated by succinic acid(SA), ninhydrin(NH), iodoacetic acid(IA) and picric acid(PA). The enzyme activities were inhibited 89%, 37%, 19%, and 15% by 0.4 mM FDNB, 0.3 mM DCCD, 0.2 mM EA and 0.15 mM CCCP, but stimulated 51%, 21%, 14% and 15% by 1.5 mM SA, 0.01 mM NH, 0.5 mM IA and 1.0 mM PA, respectively. By amino acid having the ring formed hydrophobic residues (0.1 mM proline, 0.1 mM tryptophan and 1.5 mM phenylalanine) increased the enzyme activities up to 17%, 8% and 20% but were decreased 45% and 48% by amino acids having hydrophobic and aliphatic residues (0.8 mM norleucine and 2.5 mM isoleucine), respectively. And positively charged amino acid of 1.5 mM histidine inhibited 21% of enzyme activity, negatively charged amino acid of aspartic acid did not affected. Also polared but uncharged amino acids (1.5 mM cysteine and 1.0 mM serine) increased 25% and 27% of enzyme activities, but 0.01 mM tyrosine having a hydroxyphenyl residue inhibited 50% of enzyme activity.