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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.
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.
근원섬유단백질에 관한 연구 -제3보 Troponin-Tropomyosin Complex의 변화-
양융,이용규,Yang, Ryung,Lee, Yong-Kyu 한국식품과학회 1977 한국식품과학회지 Vol.9 No.4
근원성유로 부터 근수축조절단백질들을 추출정제하고 저장중의 변화를 연구하여 다음과 같은 결과를 얻었다. 1. ${\alpha}-actinin$은 그 분자형(分子形)이나 생물활성(生物活性)에 아무런 변화도 일으키지 않았다. 2. 근육저장중에 근원섬유의 troponin-troponin complex의 함량은 감소되고 있으며 troponin-tropomyosin complex의 troponin함유비(含有比)는 낮아지고 있다. The procedures for the Preparation of regulatory proteins of myofibrill were developed and postmortem changes in the regulatory proteins of myofibrill were investigated. Both the physiological property and molecular shape of ${\alpha}-actinin$ from pre-rigor muscle did not differ from those of ${\alpha}-actinin$ from post-rigor muscle. On the other hand, although tropomyosin of myofibril changed negligibly during the post-mortem storage of muscle, troponin of myofibril changed remarkably.
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.