인삼 캘모듈린의 1차 구조

조경련,윤주억,Cho, Kyung-Ryun,Yoon, Joo-Ok 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.6

인삼 캘모듈린을 CNBr 및 arginylendopeptidase로 절단하여 펩티드 단편을 얻고, 이들 펩티드의 아미노산 서열을 분석하므로서 인삼 캘모듈린의 전 아미노산 서열을 결정하였다. 인삼 캘모듈린 단백질은 149잔기의 아미노산을 가지고 있였으며, 아미노-말단 아미노산은 아세틸화된 알라닌이었다. 인삼 캘모듈린에는 트립토판이 없었고, 1몰당 히스티딘, 티로신, 시스테인, $N_{\varepsilon}$-트리에틸리신 잔기가 각각 1몰씩 함유되고 있었다. 인삼 캘모듈린의 아미노산 서열을 소의 뇌 캘모듈린과 비교한 결과, 13잔기의 아미노산 치환과, 1잔기의 아미노산 삽입이 있었다. The complete amino acid sequence of calmodulin obtained from Panax ginseng was determined by sequencing the cyanogen bromide and arginylendopeptidase digested peptides of the purified Panax gingseng calmodulin. The calmodulin protein was found consisted of 149 amino acid residues and its amino-terminus was acetylalanine. Panax ginseng calmodulin did not contain tryptophan but contained 1 mol of histidine, tyrosine, cysteine, and $N_{\varepsilon}$-trimethyllysine residues per mol of the protein. A comparison of its amino acid sequence with that of bovine brain calmodulin indicated that there were 13 amino acid substitutions and one insertion of amino acid residues in Panax ginseng calmodulin.

인삼 캘모듈린의 1차 구조

조경련,윤주억 ( Kyung Ryun Cho,Joo Ok Yoon ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.6

The complete amino acid sequence of calmodulin obtained from Panax ginseng was determined by sequencing the cyanogen bromide and arginylendopeptidase digested peptides of the purified Panax gingseng calmodulin. The calmodulin protein was found consisted of 149 amino acid residues and its amino-terminus was acetylalanine. Panax ginseng calmodulin did not contain tryptophan but contained 1 mol of histidine, tyrosine, cysteine, and Nε-trimethyl-lysine residues per mol of the protein. A comparison of its amino acid sequence with that of bovine brain calmodulin indicated that there were 13 amino acid substitutions and one insertion of amino acid residues in Panax ginseng calmodulin.

발아 현미를 첨가한 백설기의 품질 특성

조경련 ( Kyung Ryun Cho ) 한국식품영양학회 2007 韓國食品營養學會誌 Vol.20 No.2

부추 첨가 스폰지 케이크의 품질 특성 연구

조경련 ( Kyung Ryun Cho ) 한국식품영양학회 2010 韓國食品營養學會誌 Vol.23 No.4

This study was performed to investigate the quality characteristics of sponge cake made with leek(Allium tuberosum Rottler) powder. In order to evaluate the physical and sensory properties of different cake, the leek powder was added to wheat flour at various ratios(3, 5, 7, 9%, w/w). The specificgravity of bread dough tends to increase with the addition of leek powder. The moisture levels of the sponge cakes made with leek powder were higher than that of the control. Crumb color values, lightness(L) and redness(a) decreased by leek powder addition, while yellowness(b) was significantly increased (p<0.05). In texture analyses, hardness, cohesiveness, springiness andgumminess decreased with the addition of leek powder. In sensory evaluations, the 3% leek powder sponge cake showed higher sensory property scores than others(p<0.05).

브로콜리 분말을 첨가한 설기떡의 품질 특성

조경련 ( Kyung Ryun Cho ) 韓國食品營養學會 2009 韓國食品營養學會誌 Vol.22 No.2

Physical, textural and sensory properties of Seolgiddeok prepared with different amounts of broccoli(Brassica oleracea var. italica Plen.) powder were investigated during 3 days of storage. Moisture content decreased gradually during storage and was less in broccoli powder-amended samples. The color L value decreased significantly with increasing broccoli powder, whereas both redness and yellowness increased. Texture analyses revealed that hardness, chewiness, gumminess, adhesiveness and fracturability of Seolgiddeok tended to decrease in proportion to the amount of broccoli powder in the formula. Seolgiddeok gelatinization was investigated using amylographing. Break down and setback were low in broccoli powder Seolgiddeok. Sensory evaluations revealed that, Seolgiddeok prepared with broccoli powder was superior in flavor, chewiness, softness to unamended samples. Seolgiddeok prepared with 3% broccoli powder showed the highest overall acceptability score. Use of broccoli powder in Seolgiddeok preparation improves sensory characteristics and delays retrogradation.

HIV-1 Protease Assay by the Newly Synthesized Chromophoric Peptide Substrates

윤주억,조경련,Yoon, Joo-Ok,Cho, Kyung-Ryun Korean Society for Biochemistry and Molecular Biol 1991 한국생화학회지 Vol.24 No.4

HIV-1 프로테아제의 새로운 크로모포릭 펩티드 기질로서 Asn-Asn-Gln-Val-Phe$(NO_2)$-ValArg-$NH_2$와 acetyl-Arg-Lys-Leu-Val-Phe$(NO_2)$-Leu-Asp-Gly-$NH_2$를 합성하고, 발린과 p-니트로 페닐알라닌 잔기 사이의 펩티드 결합이 가수분해됨을 알았다. 이들 합성 펩티드는 분해되면 310 nm에서의 흡광도가 감소되었다. HIV-1 프로테아제의 두 펩티드 기질의 가수분해 반응속도는 기질 턴오버수 ${\leq}$20%에서 반응시간에 비례하였다. 이들 합성기질의 용해도는 pH 4.7, 50-500 nM에서 반응 초속도 측정에 충분하였다. 또 합성한 두 펩티드 기질에 대한 정상상태에서의 효소반응이 $K_{cat}$, $K_m$, $K_{cat}/K_m$ 및 $K_i$값들을 다른 펩티드 기질에 대한 값들과 비교 검토하였다. HIV-1 protease hydrolyzed the newly synthesized peptides, Asn-Asn-Gln-Val-Phe $(NO_2)$-Val-Arg-$NH_2$ and acetyl-Arg-Lys-Leu-Val-Phe$(NO_2)$-Leu-Asp-Gly-$NH_2$ between the valyl and $({\rho}-nitro)$phenylalanyl residues. The hydrolysis of these peptides resulted in a decrease in UV absorbance at 310 nm. The HIV-1 protease-catalyzed peptidolysis of these two peptide substrates was characterized by a linear time course at substrate turnover of ${\leq}$20%. The solubilities of these substrates at pH 4.7 were sufficient to perform initial rate measurements over a concentration range of 50 to 500 nM. Steady-state kinetic data and inhibition constants of the peptidolysis of these peptide substrates resulted in comparable values.

콩 캘모듈린의 아미노산 서열

윤주억,조경련,변광의 ( Joo Ok Yoon,Kyung Ryun Cho,Kwang Eui Byoun ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.1

The complete amino acid sequence of calmodulin from soybean was determined by purifying and sequencing the cyanogen bromide and tryptic peptides. Soybean calmodulin consisted of 148 amino acid residues and its aminoterminus was blocked with an acetyl group. This calmodulin lacked tryptophan and contained one mol each of N ?trimethyllysine, histidine, and cysteine residues and two moles of tyrosine residues per mol of the protein. The comparison of the amino acid sequence of soybean calmodulin with that of bovine brain calmodulin indicated that there were nine amino acid substitutions other than amide assignments, one insertion and one deletion of amino acid residues in soybean calmodulin.

새롭게 합성한 크로모포릭 펩티드 기질에 의한 HIV - 1 프로테이자에의 효소반응속도 측정

윤주억,조경련 ( Joo Ok Yoon,Kyung Ryun Cho ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.4

HIV-1 protease hydrolyzed the newly synthesized peptides, Asn-Asn-Gln-Val-Phe (NO₂)-Val-Arg-NH₂ and acetyl-Arg-Lys-Leu-Val-Phe(NO₂)-Leu-Asp-Gly-NH₂ between the valyl and (p-nitro)phenylalanyl residues. The hydrolysis of these peptides resulted in a decrease in UV absorbance at 310 nm. The HIV-1 protease-catalyzed peptidolysis of these two peptide substrates was characterized by a linear time course at substrate turnover of ≤20%. The solubilities of these substrates at pH 4.7 were sufficient to perform initial rate measurements over a concentration range of 50 to 500 nM. Steady-state kinetic data and inhibition constants of the peptidolysis of these peptide substrates resulted in comparable values.

Amino Acid Sequence of Calmodulin from Soybean

윤주억,조경련,변광의,Yoon, Joo-Ok,Cho, Kyung-Ryun,Byoun, Kwang-Eui 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.1

정제한 콩 캘모듈린으로부터 CNBr 및 트럽신 펩티드를 얻고, 이들의 아미노산 서열을 분석하므로서 콩 캘모듈린의 전 아미노산 서열을 결정하였다. 콩 캘모듈린은 148개의 아미노산 잔기를 가졌으며, 아미노-말단 잔기는 아세틸화된 알라닌이었다. 또 트립토판이 결핍되어 있었고, 이 단백질 한 몰에는 N-트리메틸리신, 히스티딘, 시스턴이 각각 한 몰, 티로신은 두 몰이 함유되어 있었다. 콩 캘모듈린의 아미노산 서열을 소의 뇌 캘모듈린과 비교한 결과, 9가지 아미노산 잔기가 치환되어 있었고, 새롭게 삽입된 것과 빠져 없어진 것이 각각 한 잔기씩 있었다. The complete amino acid sequence of calmodulin from soybean was determined by purifying and sequencing the cyanogen bromide and tryptic peptides. Soybean calmodulin consisted of 148 amino acid residues and its aminoterminus was blocked with an acetyl group. This calmodulin lacked tryptophan and contained one mol each of N-trimethyllysine, histidine, and cysteine residues and two moles of tyrosine residues per mol of the protein. The comparison of the amino acid sequence of soybean calmodulin with that of bovine brain calmodulin indicated that there were nine amino acid substitutions other than amide assignments, one insertion and one deletion of amino acid residues in soybean calmodulin.

캘모듈린 cDNA 의 합성과 발현

윤주억,조경련,김성기 ( Joo Ok Yoon,Kyung Ryun Cho,Sung Kih Kim ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.3

A calmodulin cDNA was designed and synthesized from 61 chemically synthesized oligonucleotides using the method of enzymatic ligation and overproduced in Escherichia coli for the purpose of developing recombinant DNA approaches to study strucure-function relationships in this calcium-binding regulatory protein. The recombinant protein isolated from E. coli functions as a calmodulin in properties that were assayed: calcium binding and calcium-dependent conformational change. The initiating methionine was removed by E. coli leaving alanine as the first amino acid, as in the naturally occurring calmodulins. The first amino acid was not acetylated, but this difference from the higher plant and vertebrate calmodulins has no apparent effect on the function. The recombinant calmodulin also lacks posttranslational modification: a N^ε, N^ε, N^ε-trimethyllysine at position 115. The recombinant calmodulin was found to activate NAD kinase to a maximal level that was at least 3.8-fold higher than that obtained with soybean calmodulin. The lack of methylation of lysine-115 may contribute to the maximal level of NAD kinase activation.