3-deoxyglucosone에 의한 단백질의 중합

양융,신동범,신완철,오상환,Yang, Ryung,Shin, Dong-Bum,Shin, Wan-Chul,Oh, Sang-Hwan 생화학분자생물학회 1990 한국생화학회지 Vol.23 No.3

pH 7.4, $37^{\circ}C$의 생리적 반응조건에서 HSA, ovalbumine, BSA, lysozyme, RNase A 및 IgG와 3-deoxyglucosone을 반응시키고 단백질의 중합현상과 아미노산 잔기의 손상상태를 연구하였다. 3-deoxyglucosone은 모든 단백질을 중합시킬 수 있으나 특히 lysozyme, RNase A 및 IgG를 현저하게 중합시켰다. 또한 arginine 잔기를 크게 손상시켰다. glucose에 의한 단백질의 중합과정은 glucose가 단백질의 아미노 그룹과의 반응으로 3-deoxyglucosone을 형성시키고, 이것이 단백질의 lysine 잔기와 arginine 잔기를 공격하여 cross link를 형성시키는 것으로 추정되었다. Human serum albumin, bovine serum albumin, ovalbumin, IgG, lysozyme and ribonuclease A were reacted with 3-deoxyglucosone under physiological conditions of $37^{\circ}C$ and pH 6.4, and polymerization of proteins and the impairments of amino acid residues were investigated. Proteins tested, especially lysozyme, IgG and ribonuclease A, were polymerized significantly, and lysine residue and arginine residue, especially arginine residue of proteins, were impaired remarkable. Experimental results strongly suggested that 3-deoxyglucosone, formed from proteins-glucose reaction system, was the corss-linker responsible for the polymerization of proteins.

환원당에 의한 생체단백질의 Glycosylation

양융,신동범,신완철,오상환 ( Ryung Yang,Dong Bum Shin,Wan Chul Shin,Sang Hwan Oh ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.4

In order to get further informations on the loss of biologic function by the nonenzymatic reaction of glucose with proteins, reducing sugars (glucose, fructose, galactose, mannose, ribose and xylose) were reacted with proteins (bovine serum albumin, lysozyme, ovalbumin, RNase A) in 0.2 M phosphate buffer (pH 7.4) at 37℃, and polymerization of proteins and changes in amino acid composition were compared. Proteins tested were polymerized and some amino acid residues were impaired significantly by Maillard reaction. The degree of polymerization and impairment of amino acid residues, however, were different, depending on the kinds of proteins and reducing sugars.

3 - deoxyglucosone 에 단백질의 중합

양융,신동범,신완철,오상환 ( Ryung Yang,Dong Bum Shin,Wan Chul Shin,Sang Hwan Oh ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.3

Human serum albumin, bovine serum albumin, ovalbumin, IgG, lysozyme and ribonuclease A were reacted with 3-deoxyglucosone under physiological conditions of 37℃ and pH 6.4, and polymerization of proteins and the impairments of amino acid residues were investigated. Proteins tested, especially lysozyme, IgG and ribonuclease A, were polymerized significantly, and lysine residue and arginine residue, especially arginine residue of proteins, were impaired remarkable. Experimental results strongly suggested that 3-deoxyglucosone, formed from proteins-glucose reaction system, was the corss-linker responsible for the polymerization of proteins.

환원당 - 단백질 반응계로부터의 dicarbonyl 화합물의 생성

신동범,양융,신완철,오상환 ( Dong Bum Shin,Ryung Yang,Wan Chul Shin,Sang Hwan Oh ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.3

When proteins (bovine serum albumin, RNase A and lysozyme) were reacted with glucose or fructose under physiological conditions of 37℃ and pH 7.4, proteins were polymerized and also the amino acid residues of proteins were impaired. These phenomena were considered to be due to the formation of dicarbonyl compound from protein-sugar reaction systems, and therefore dicarbonyl compounds liberated were identified quantitatively by thin layer chromatography and mass spectrometry. 3-deoxyglucosone was the main product among dicarbonyl compounds.

환원당-단백질 반응계로부터의 dicarbonyl 화합물의 생성

신동범,양융,신완철,오상환,Shin, Dong-Bum,Yang, Ryung,Shin, Wan-Chul,Oh, Sang Hwan 생화학분자생물학회 1990 한국생화학회지 Vol.23 No.3

pH 7.4, $37^{\circ}C$의 생리적 반응조건에서 단백질(bovine serum albumin, RNase A 및 lysozyme)을 glucose 또는 fructose와 반응시켰을 때, 단백질은 중합현상을 나타내었을 뿐만 아니라 아미노산 잔기도 크게 손상되었다. 이러한 현상들은 반응계로부터의 dicarbonyl 화합물의 생성과 관련이 깊은 것으로 관찰되어 dicarbonyl 화합물을 정량적으로 동정하였다. TLC와 mass spectrometry에 의하여 동정된 dicarbonyl 화합물로는 3-deoxyglucosone, glyoxal. methyl glyoxal 이었으며, 3-deoxyglucosone이 주된 생성물이었다. When proteins (bovine serum albumin, RNase A and lysozyme) were reacted with glucose or fructose under physiological conditions of $37^{\circ}C$ and pH 7.4, proteins were polymerized and also the amino acid residues of proteins were impaired. These phenomena were considered to be due to the formation of dicarbonyl compound from protein-sugar reaction systems, and therefore dicarbonyl compounds liberated were identified quantitatively by thin layer chromatography and mass spectrometry. 3-deoxyglucosone was the main product among dicarbonyl compounds.

Glucose-protein 반응계로부터의 3-deoxyglucosone의 생성

신동범,양융,오상환 연세대학교 산업기술연구소 1990 논문집 Vol.22 No.1

pH 7.4, 37℃의 생리적 반응조건에서 단백질(bovine serum albumin, RNase A 및 lysozyme)을 glucose 또는 fructose와 반응시켰을 때, 단백질은 중합현상을 나타내었을 뿐만 아니라 아미노산 잔기도, 크게 손상되었다. 이러한 현상들은 반응계로부터의 dicarbonyl 화합물의 생성과 관련이 깊은 것으로 관찰되어 dicarbonyl 화합물을 정량적으로 동정하였다. TLC 와 mass spectrometry에 의하여 동정된 dicarbonyl 화합물로는 3-deoxyglucosone, glyoxal, methyl glyoxal이었으며, 3-deoxyglucosone이 주된 생성물이었다. When proteins (bovine serum albumin. RNase A and lysozyme) were reacted with glucose or fructose under physiological conditions of 37℃ and pH 7.4, proteins were polymerized and also the amino acid residues of proteins were impaired. These phenomena were considered to be due to the formation of dicarbonyl compound from protein-sugar reaction systems, and therefore dicarbonyl compounds liberated were identified quantitatively by thin layer chromatography and mass spectrometry. 3-deoxyglucosone was the main product among dicarbonyl compounds.

환원당과 단백질의 마이얄 반응

양융,신동범,오상환 연세대학교 산업기술연구소 1990 논문집 Vol.22 No.1

Glucose에 의한 생체단백질의 기능저하에 대한 정보를 얻기 위하여 생리적 조건에 가까운 반응조건(0.2M sodium phosphate buffer, pH 7.4 37℃)에서 생체단백질과 환원당을 반응시키고, 그에 따른 단백질의 중합현상과 아미노산의 손상정도를 비교하였다. 환원당에 의한 비효소적 glycosylation(Maillard reaction)은 단백질을 중합시킬 뿐만 아니라 아미노산 잔기를 크게 손상시켰다. 그러나, 단백질의 중합도와 아미노산의 손상정도는 단백질의 종류는 물론 환원당의 종류에 따라 차이가 있었다. In order to get further informations on the loss of biologic function by the nonenzymatic reaction of glucose with proteins, reducing sugars were reacted with proteins in 0.2M phosphate buffer(pH 7.4) at 37℃, and polymerization of proteins and changes in amino acid composition were compared. Proteins tested were polymerized and some amino acid residues were impaired significantly by Maillard reaction. The degree of polymerization and impairment of amino acid residues, however, were different, depending on the kinds of proteins and reducing sugars.

성숙한 Longissimus Dorsi근과 Soleus근의 근원섬유단백질의 특성비교

양융,최혁준,윤창훈,신완철,오상환 한국노화학회 1991 한국노화학회지 Vol.1 No.1

3-deoxyglucosone에 의한 단백질의 modification

신동범,오상환,양융 연세대학교 산업기술연구소 1990 논문집 Vol.22 No.1

pH 7.4, 37℃의 생리적 반응조건에서 HSA, ovalbumine, BSA, lysozyme, RNase A 및 IgG와 3-deoxyglucosone을 반응시키고 단백질의 중합현상과 아미노산 잔기의 손상상태를 연구하였다. 3-deoxyglucosone은 모든 단백질을 중합시킬 수 있으나 특히 lysozyme, RNase A 및 IgG를 현저하게 중합시켰다. 또한 Arginine잔기를 크게 손상시켰다. glucose에 의한 단백질의 중합과정은 glucose가 단백질의 아미노 그룹과의 반응으로 3-deoxyglucosone을 형성시키고, 이것이 단백질의 lysine 잔기와 arginine 잔기를 공격하여 cross link를 형성시키는 것으로 추정되었다. Human serum albumin, bovine serum albumin, ovalbumin, IgG, lysozyme and ribonuclease A were reacted with 3-deoxyglucosone under physiological conditions of 37℃ and pH 7.4, and polimerization of proteins and impairments of amino acid residues were investigated. Proteins tested, especially lysozyme, IgG and ribonuclease A, were polymerized significantly, and lysine residue and arginine residue, espectially arginine residue of proteins were impaired remarkably. Experimental results strongly suggested 3-deoxyglucosone, formed from proteins-glucose reaction system, was the cross-linker responsible for the polymerization of proteins.