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연어(Salmo Salar) 알중의 Carboxypeptidase A의 분리정제 및 그 성질에 관한 연구
김준행,이갑득,민태진,Kim, Joon-Haeng,Lee, Kap-Duk,Min, Tae-Jin 생화학분자생물학회 1986 한국생화학회지 Vol.19 No.3
야생 연어 알중의 carboxypeptidase A를 CM-cellulose, $(NH_4)_2SO_4$ 분별침전, DEAE-cellulose column chromatography 및 sephadex G-75 겔 여과로 정제하여, 그 특성을 조사하였다. 활성분획 A는 기질 bovine hemoglobin 및 hippuryl-L-phenylalanine에 대하여 활성을 보였다. 이 효소의 분자량은 44,000 dalton이었으며, 18종의 서로 다른 아미노산으로 구성되어 있는 단량체였다. 최적 pH는 4.5, 최적 온도는 $60^{\circ}C$ 였고, pH 2.5~5.5, $20^{\circ}C{\sim}60^{\circ}C$에서 30분간 안정하였다. 이 효소는 glycyl-L-phenylalanine의 펩티드 결합을 분해시키는 특이성을 보였으며, $K_m$ 값은 0.29 mM이었다. 효소활성은 $Zn^{2+}$, $Fe^{3+}$, 및 L-cysteine에 의하여 억제되었으며, L-cysteine은 경쟁적 억제인자였고, 그 $K_i$ 값은 1.2 mM이었다. The enzymic properties of carboxypeptidase A in the eggs of salmon (Salmo salar) were investigated by purification with CM-cellulose, ammonium sulfate fractionation, DEAE-cellulose, and sephadex G-75 gel filtration. The fraction A showed its activity toward substrate such as bovine hemoglobin and hippuryl-L-phenylalanine. The molecular weight of this enzyme was determined to be 44,000 daltons by SDS-PAG electrophoresis and the enzyme was monomeric protein composed of 18 different amino acids. Optimum pH was 4.5, optimum temperature was $60^{\circ}C$, and the enzyme was stable at pH 2.5-5.5 and $20^{\circ}C-60^{\circ}C$. This enzyme showed substrate specificity hydrolyzing the peptide bond of glycyl-L-phenylalanine. Its $K_m$ value was 0.29 mmol and the enzyme was inhibited by $Zn^{2+}$, $Fe^{3+}$, and L-cysteine. The L-cysteine was found to be competitive inhibitor, and its $K_i$ value was determined to be 1.2 mmol by Dixon plot.
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야생연어(Salmo Salar) 알 중의 Carboxypeptidase A 의 특성에 관한 연구
김준행,민태진 동국대학교 자연과학연구소 1985 자연과학연구 논문집 Vol.5 No.-
야생 연어알중의 carboxypeptidase A를 CM-cellulose, (NH₄)SO₄ 0.5포화, DEAE-cellulose column 크로마토그라피 및 Sephadex G-75 겔 여과에 의하여 분리 정제하여, 그 특성을 조사하였다. 야생 연어알로부터 2종류의 활성분획 A 및 B를 얻었다. 활성분획 A는 bovine hemoglobin 및 hippuryl-L-phenylalanine과 같은 기질에 대하여 활성을 보였다. 이 효소의 분자량은 44,000 dalton이었으며, 18종의 아미노산으로 구성되여 있는 단량체였다. 최적 pH는 4.5, 최적 온도는 60℃였고, pH2.5~3.5, 20~60℃에서 안정하였다. 이 효소는 glycyl-L-phenylalanine의 펩티드 결합을 분해시키는 특이성을 보였으며, Km값은 0.29mM이였다. Fe³및 L-cysteine에 의하여 저해받았으며, L-cysteine은 경쟁적 저해제였고, 그의 Ki값은 1.2mM이였다. The enzymic properties of Carboxypeptidase A in the Eggs of Salmon (Salmo Salar) were investigated by purification with CM-cellulose, ammonium sulfate fractionation (50%), DEAE-cellulose and Sephadex G-75 gel filtration. Two kind of active fraction A and B were isolated from the egg of wild salmon. The fraction A showed its activity toward substrate such as bovine hemoglobin and hippuryl-L-phenylalanine. The molecular weight of this enzyme was determined to be 44,000 daltons by SDS-PAG electrophoresis and the enzyme was monomeric protein composed of 18 amino acids. Optimum pH was 4.5, optimum temperature was 60℃, and the enzyme was stable at PH 2.5~3.5 and 20℃-60℃ This enzyme showed substrate specificity hydrolyzing the peptide bond of glycyl-L-phenylalanine. Its Km value was 0.29 mM and the enzyme was ingibited by Zn, Fe and L-cysteine. The L-cysteine was found to be competitive inhabitor, and its Ki value was determined to be 1,2 mM by Dixon plot.
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연어 ( Salmo Salar ) 알중의 Carboxypeptidase A의 분리정제 및 그 성질에 관한 연구
이갑득,민태진,김준행 생화학분자생물학회 1991 BMB Reports Vol.19 No.3
The enzymic properties of carboxypeptidase A in the eggs of salmon (Salmo solar) were investigated by purification with CM-cellulose, ammonium sulfate fractionation, DEAF-cellulose, and sephadex G-75 gel filtration. The fraction A showed its activity toward substrate such as bovine hemoglobin and hippuryl-L-phenylalanine. The molecular weight of this enzyme was determined to be 44,000 daltons by SDS-PAG electrophoresis and the enzyme was monomeric protein composed of 18 different amino acids. Optimum pH was 4.5, optimum temperature was 60℃, and the enzyme was stable at pH 2.5-5.5 and 20°-60℃. This enzyme showed substrate specificity hydrolyzing the peptide bond of glycyl-L-phenylalanine. Its K_m value was 0.29 mmol and the enzyme was inhibited by Zn^(2+), Fe^(3+), and L-cysteine. The L-cysteine was found to be competitive inhibitor, and its K_i value was determined to be 1.2 mmol by Dixon plot.
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