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$Chitinase/{\beta}-1,3-glucanase$ 활성 동시보유 벼잎단백질 분획의 성질
엄성연,김수일,Uhm, Sung-Yon,Kim, Su-Il 한국응용생명화학회 1993 Applied Biological Chemistry (Appl Biol Chem) Vol.36 No.5
벼잎의 산성 buffer(pH 2.8) 추출 조효소는 5개의 전기영동 band들이 PR protein으로 알려진 chitinase와 ${\beta}-1,3-glucanase$의 효소활성을 보유하고 있는 것으로 나타났다. 조효소는 DEAE-cellulose 및 chitin affinity chromatography로 염기성 및 산성 효소군으로 분획되었으며, 이들은 두 효소활성이외에도 lysozyme 활성을 보유하고 있었다. 분자량이 $14.3{\sim}66.0\;kd$ 범위인 이 두 효소군이 보유한 각 효소활성의 최적 pH와 온도를 조사해본 결과,${\beta}-1,3-glucanase$는 각각 pH 5와 $60^{\circ}C$로 동일하였으나, chitinase는 염기성 효소군에서 pH 4와 $50^{\circ}C$, 산성 효소군에서는 pH 3와 $60^{\circ}C$으로 다르게 나타나서, 전기영동 양상과 더불어 서로 상이한 효소분획인 것으로 추정되었다. Five electrophoretic bands of crude enzyme extracted from rice leaves were found to possess both chitinase and ${\beta}-1,3-glucanase$ activities. These $chitinase/{\beta}-1,3-glucanase$ were resolved into acidic and basic fractions of protein by DEAE-cellulose and chitin affinity column chromatography. The optimal pH and temperature for ${\beta}-1,3-glucanase$ activity of two fractions were in the same extent as pH 5 and $60^{\circ}C$, whereas those for chitinase activity differed from one another; pH 3 and $60^{\circ}C$ for the acidic and pH 4 and $50^{\circ}C$ for the basic fraction, respectively. In addition, lysozyme activity was found in both fractions.
Chitinase, ${\beta}-1,3-glucanase$ 및 lysozyme 효소활성을 보유한 벼잎 산성단백질 RCG-2
엄성연,김수일,Um, Sung-Yon,Kim, Su-Il 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.1
벼잎의 산성용액 추출물로부터 ion exchange chromatography chitin affinity chromatography chromatofocusing gel slicing 등의 방법으로 단백질 RCG-2를 순수분리하였다. 본 단백질은 chitin과 laminarin을 가수분해하므로 chitinase와 ${\beta}-1,3-glucanase$ 활성을 함께 보유하고 있는 것으로 나타났으며, 이외에도 M. lysodeiktikus cell wall을 가수분해하는 lysozyme 활성도 보유하는 것으로 판명되었다. 분자량이 29.77 kd인 본 효소의 chitinase 활성은 pH 4.0에서, ${\beta}-1,3-glucanase$ 활성은 pH 7.0에서 최대로 나타났고, 최적온도는 두 효소 활성 모두 $40^{\circ}C$ 이었다. chitin에 대한 $K_M$ 값은 7.86 mM, $V_{max}$는 $0.025\;{\mu}M/min$, laminarin $({\beta}-1,3-glucan)$에 대한 것은 각각 5.95 mM, $0.16{\mu}\;M/min.$ 이었으며, 정제된 효소는 chitin을 chitooligosaccharide로 분해하는 것으로 나타나서 endochitinase로 판명되었다. An acidic protein, RCG-2, containing chitinase and ${\beta}-1,3-glucanase$ activity conccurrently was purified from rice leaves by chromatofocusing and gel slicing. The purified enzyme gave a single band on polyacrylamide gel electrophoresis and its molecular weight was appeared to be 29.7 kd using SDS-PAGE. This enzyme also had lysozyme activity. The optimal temperature for both enzyme activities was $40^{\circ}C$, optimal pH were 4.0 for chitinase activity and 7.0 for ${\beta}-1,3-glucanase$ activity. $K_M$ and $V_{max}$ values for chitinase were 7.86 mM and $0.025\;{\mu}M/min.$, and those for ${\beta}-1,3-glucanase$ were 5.95 mM and $0.16\;{\mu}M/min.$ respectively. TLC analysis of the enzyme hydrolysates of chitooligosaccharides indicated that this enzyme acts as endochitinase.
Chitooligosaccharides 처리에 의해 유도되는 chitinase, ${\beta}-1,3-glucanase$ 활성 보유 벼 염기성 단백질 ICG의 분리 및 성질
엄성연,박희영,김수일,Um, Sung-Yon,Park, Hee-Young,Kim, Su-Il 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.1
A basic inducible protein, ICG, containing chitinase and ${\beta}-1,3-glucanase$ activity concomittantly was purified from cell suspension culture media of rice after the treatment of chitooligosaccharides. The isolated ICG enzyme gave a single band on native and SDS polyacrylamide gel electrophoresis and its molecular weight was estimated to be 52.53 kd. The optimal temperature and optimal pH of both enzyme activities in ICG were $60^{\circ}C$, pH 6.0 for chitinase activity and $37^{\circ}C$, pH 4.0 for ${\beta}-1,3-glucanase$ activity. $K_M$ and $V_{max}$ values for chitinase were 0.474 mM. 2.997 nM/min., and those for ${\beta}-1,3-glucanase$ were 1.004 mM 0.739 nM/min. respectively. TLC analysis of the chitooligosaccharide hydrolysates with ICG enzyme indicated that ICG acts as endochitinase. 벼 세포 현탁배양여액으로부터 chitooligosaccharides에 의해 유도된 염기성 단백질 ICG를 순수분리하였다. 본 단백질은 chitin과 laminarin을 가수분해하므로 chitinase와 ${\beta}-1,3-glucanase$ 활성을 함께 보유하고 있는 것으로 나타났으며, 벼잎 단백질 RCG-2와는 달리 lysozyme 활성을 가지고 있지 않았다. 분자량이 52.53 kd인 본 효소의 chitinase 활성은 pH 5.0, $60^{\circ}C$, ${\beta}-1,3-glucanase$ 활성을 pH 4.0, $40^{\circ}C$의 조건에서 최대로 나타났다.$NAG_5$에 대한 $K_M$ 및 $V_{max}$ 수치는 각각 0.474 mM, 2.997 nM/min., laminarin에 대한 것은 각각 1.004 mM, 0.739 nM/min.로 나타나, ICG는 RCC-2보다 높은 기질친화성을 가지고 있으며 chitin을 chitooligosaccharide로 분해하는 endo형 chitinase로 판명되었다.
Chitooligosaccharides 처리에 의해 유도되는 chitinase , β - 1,3 - glucanase 활성 보유 벼 염기성 단백질 ICG 의 분리 및 성질
엄성연(Sung Yon Um),박희영(Hee Young Park),김수일(Su Il Kim) 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.1
A basic inducible protein, ICG, containing chitinase and β-1,3-glucanase activity concomittantly was purified from cell suspension culture media of rice after the treatment of chitooligosaccharides. The isolated ICG enzyme gave a single band on native and SDS polyacrylamide gel electrophoresis and its molecular weight was estimated to be 52.53 kd. The optimal temperature and optimal pH of both enzyme activities in ICG were 60C, pH 6.0 for chitinase activity and 37℃, pH 4.0 for β-1,3-glucanase activity. K_M and V_(max) values for chitinase were 0.474 mM. 2.997 nM/min., and those for β-1,3-glucanase were 1.004 mM·0.739 nM/min. respectively. TLC analysis of the chitooligosaccharide hydrolysates with ICG enzyme indicated that ICG acts as endochitinase.
Chitinase / β - 1,3 - glucanase 활성 동시보유 벼잎단백질 분획의 성질
엄성연(Sung Yon Uhm),김수일(Su Il Kim) 한국응용생명화학회 1993 Applied Biological Chemistry (Appl Biol Chem) Vol.36 No.5
Five electrophoretic bands of crude enzyme extracted from rice leaves were found to possess both chitinase and β-1,3-glucanase activities. These chitinase/β-1,3-glucanases were resolved into acidic and basic fractions of protein by DEAF-cellulose and chitin affinity column chromatography. The optimal pH and temperature for β-1,3-glucanase activity of two fractions were in the same extent as pH 5 and 60℃, whereas those for chitinase activity differed from one another; pH 3 and 60℃ for the acidic and pH 4 and 50℃ for the basic fraction, respectively. In addition, lysozyme activity was found in both fractions.
Chitinase , β - 1,3 - glucanase 및 lysozyme 효소활성을 보유한 벼잎 산성단백질 RCG - 2
엄성연(Sung Yon Um),김수일(Su Il Kim) 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.1
An acidic protein, RCG-2, containing chitinase and β-1,3-glucanase activity conccurrently was purified from rice leaves by chromatofocusing and gel slicing. The purified enzyme gave a single band on polyacrylamide gel electrophoresis and its molecular weight was appeared to be 29.7 kd using SDS-PAGE. This enzyme also had lysozyme activity. The optimal temperature for both enzyme activities was 40℃, optimal pH were 4.0 for chitinase activity and 7.0 for β-1,3-glucanase activity. K_M and V_(max) values for chitinase were 7.86 mM and 0.025 μM/min., and those for β-1,3-glucanase were 5.95 mM and 0.16 μM/min. respectively. TLC analysis of the enzyme hydrolysates of chitooligosaccharides indicated that this enzyme acts as endochitinase.