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.

근육에 있어서의 화학에너지의 기계에너지로의 변환속도에 관한 비교 연구

양융 연세대학교 산업기술연구소 1985 논문집 Vol.17 No.1

To compare the conversion rate of chemical energy to mechanical energy in muscle, myofibrillar proteins were prepared from various mammalian muscles, fish muscle and molluscan muscles, and physico-chemical characteristics of myofibrillar proteins were compared one another. Differences in ATPase activity, trypsin digestibility and protein composition of myofibril were observed, although the morphological characteristics of myofibril and the sedimentation constants of myosin did not vary from muscle to muscle.

닭고기의 과학

양융 대한양계협회 1974 월간 양계 Vol.6 No.11

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.

식품냉동의 문제점

양융 한국식품산업협회 1975 좋은식품 Vol.27 No.-

小麥粉의 加工適性 改良에 關한 硏究

梁隆 연세대학교 대학원 1977 延世論叢 Vol.14 No.2

The effect of flour improving agent on the rheological property of wheat flour was investigated by A.A.C.C. method. Nine kinds of flour improving agent, divided into three groups, i. e, acidic inorganic polymer, biopolymer and polysaccharide, were added to flour, and dough was prepared. Then, changes in farinographic characteristics and extensographic characteristics of dough were measured and compared one another. 1. When sodium polyacrylate and sodium polyphosphate, which are acidic polymer electrolytes, were added to flour, sodium polyacrylate increased the valorimeter value of dough remarkably, while sodium polyphosphate increased markedly the energy value of dough. Thus, it was assumed that the rheological property of dough could be improved considerably when the mixture of polyacrylate and polyphasphate were added to flour. When potassium bromate, a strong oxidizing agent, was added to flour, the energy value of dough was enhanced remarkably, but the valorimeter value of dough did not change noticably. From this result, it was suggested that the increase in the valorimeter value of dough was not attributed entirely to the disulfide bond formation in gluten by the treatment of potassium bromate, but partly. 2. When gelatin or sodium caseinate was added to flour, the valorimeter value of dough increased negligibly. When gluten was added, however, the valorimeter value of dough increased gradually, as the content of gluten in dough was increased. From the results described above, it was considered that the improvement of rheological property of dough would be hardly obtained by the addition of fibrous protein, which is lacking in the reactive sulfhydryl group, even though the protein is a reactive biopolymer with lots of functional groups. 3. When polysaccharides, such as CMC, alginate and guar gum, were added to flour, noticeable increases in the calorimeter value and in energy value of dough was not observed. The water holding capacity of dough, however, was increased remarkably by the addition of the polysaccharides. Although the strict interaction of polysacchardes to dough components remains unclear, it is likely that the polysacchardes interacts with dough components through the formation of hydrogen bond. Accordingly, it may be considered that the increase in the valorimeter value of dough is not attributed entirely to the formation of hydrogen bond between dough components and flour improving agents. The result that water holding capacity of dough was enhanced by the addition of polysaccharide may be interpreted to be attributed to the characteristics of polyhydroxyl polymer, that is, a strong hydrophilic property.

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.

乳製品과 肉加工品의 品質水準

梁隆 한국식품과학회 1986 식품과학과 산업 Vol.19 No.4

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.

Malate dehydrogenase의 조직특성에 관한 연구

양융,최진길 연세대학교 대학원 1990 延世論叢 Vol.26 No.1

Abstract Malate dehydrogenase was extracted from cardiac muscle and skeletal muscle, and biochemical characteristics were compared each other. Results obtained are summarized as follow : 1. Malate dehydrogenase activity in cardiac muscle was 2.80 times as high as that of skeletal muscle. 2. The content of cytoplasmic malate dehydrogenase was higher than that of mitochondrial palate dehydrogenase of cardiac muscle and skeletal muscle. 3. Malate dehydrogenase of cardiac muscle was more thermostable than that of skeletal muscle. Thermostability of cytoplasmic malate dehydrogenase was more stable than that of mitochondrial palate dehydrogenase. 4. The Km value of mitochondrial malate dehydrogenase showed high affinity for malate, while Km value of cytoplasmic malate dehydrogenase showed high affinity for oxaloacetate. 5. Distribution of surface charge between cytoplasmic and mitochondrial malate dehydrogenase was different from each other. Molecular weight of malate dehydrogenase subunit was 35,000.