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변재형,남택정 한국수산학회 1981 한국수산과학회지 Vol.14 No.1
Protein compositions of filefish (Navodon modestus) skeletal muscle and their changes in postmortem with reference to freshness kept at 0�� were investigated. The muscle protein was approximately composed of 31% sarcoplasmic, 55% myofibrillar, 10% residual intracellular, and 4% stroma protein. The sarcoplasmic and myofibrillar protein decreased while the residual intracellular protein increased with the decline of freshness during post-mortem lapse. In the analysis of electrophoretograms and its densitograms, the myofibrillar protein resembled to other fishes in protein composition: 70% actin and myosin, 20% regulatory proteins, and 10% unknown proteins. And most of the residual intracellular protein was estimated as myofibrillar protein. Troponin T, troponin C and myosin light chain 2 of the myofibrillar protein constituents were decreased during storage. Amino acid composition of the protein from the at-death muscle was similar to those of other fishes except that tryptophan and whereas leucine, isoleucine and phenylalanine were slightly increased in the protein from the muscle lapsed of 18 days. In free amino acid composition, alanine, glycine, lysine, nd especially taurine were rich in the at-death muscle. The muscle lapsed of 18 days showed an increase of taurine, histodine, valine and methionine, and a decrease of lyasine, arginine, aspartic acid, threonine, leucine, and isoleucine.
어류의 조직중에 분포하는 알카리성 단백질분해효소의 활성조건
변재형,남택정 한국수산학회 1983 한국수산과학회지 Vol.16 No.2
Quality changes of the precooked frozen sardine(Sardinops melanosticta) during frozen storage were investigated by measuring extractable protein, expressible drip, available lysine and lipid oxidation as peroxide value. Fresh sardine was dressed, washed in chilled water, cooked in boiling water to have 55℃ and 70℃ at the center of the body, frozen at -40℃, and finally stored at -20℃ for 84 days. The quality factor mentioned above were determined in both ordinary and dark muscle at 14 day intervals through the period of storage. When cooked at 70℃, the changes in expressible drip were less than that of raw and the one cooked at 55℃. In observation of the extractability of muscle protein, no great change in extractable sarcoplasmic protein was observed, the extractable myofibrillar protein, however, showed a tendency to decrease during the period of frozen storage, accompanying the increase of the alkali-soluble protein. That was more excessive in ordinary muscle than dark muscle. Lipid oxidation of dark muscle was faster than that of ordinary muscle. Acid value was not changed, and peroxide value of the samples cooked at 70℃ and 55℃ was higher than that of raw at the early stage of the storage, after 40-50 day storage, it became lower than that of raw muscle.
변재형,황혜정,남택정 한국수산학회 2000 한국수산과학회지 Vol.33 No.6
알길산은 3T3-Ll 세포의 분화를 억제하였다. 3T3-Ll 세포의 분화를 촉진시키는 인자로 밝혀진 IGF-I과 insulin을 이용하여 알긴산의 분화에 미치는 영향을 검토한 결과, 알긴산은 insulin의 분화촉진작용을 특이적으로 억제하였다. 본 연구는 알긴산을 이용하여 알긴산의 지질 감소효과를 세포의 수준에서 검증하고자 하였다는 점에서 그 의의가 있으며, 이에 알긴산의 분화억제효과가 일어나는 메카니즘에 관한 연구가 있어야 할 것으로 생각된다. This study examines the effects of alginic acid, a source of dietary fiber, in a glucose-derived media. In particular, we examined how the presence or absence of alginic acid affected the differentiation and triglyceride densities of 3T3-Ll cells. We established that the addition of insulin-like growth factor-I (IGF-I) to 3T3-Ll cells results in acceleration of differentiation. We sought to determine the role of alginic acid in the production of fat, by adding alginic acid to 3T3-Ll cells and examining its ability to limit or potentiate this stimulatory effects of IGF-I and IGF binding proteins. We have determined that alginic arid restricts 3T3-Ll cell differentiation and the creation of triglycerides, effectively attenuating 3T3-L1 cell metablolism and growth.
변재형,정보영,황금소 한국수산학회 1976 한국수산과학회지 Vol.9 No.4
魚類加工品中에 分布하는 2級 amine의 生成 原因을 究明하기 위한 硏究의 一部로서, 멸치를 22%의 食鹽을 添加하여 17℃와 27℃의 溫度別로 熟成시키면서 熟成 日程別로 蛋白質과 TMAO의 分解生成物을 分析하여 2級 amino의 生成과 關係있는 몇가지 實驗結果를 얻었기에 報告한다. 蛋白熊 窒素는 17℃와 27℃에서 熟成시켰을때, 全熟成期間을 通하여 一律的으로 減少하는 傾向을 보였으나, 아미노態 窒素는 蛋白態 窒素의 減少에 反比例하여 增加하였으며, 이 때 아미노態 窒素의 增加速度는 27℃에서 熟成한 것이 17℃에서 熟成한 것에 比하여 훨씬 빨랐다. TMA는 TMAO의 減少와 더불어 增加하여 갔으며 熟成 69日까지는 繼續 增加하다가 以後 徐徐히 減少하는 傾向을 보였다. 이때 溫度에 의한 差異는 보이지 않았다. DMA는 17℃에서 熟成시켰을 때는 熟成 69日까지 繼續 增加하다가 以後 微微한 變化를 보였으며, 27℃에서 熟成시킨 것은 熟成 59日까지는 繼續 增加하다가 그 以後는 微微한 變化를 보였다. DMA는 TMAO의 量的變化에 비추어, 17℃에서 熟成시켰을 때는 相關係數 r=-0.811, 그리고 27℃에서 熟成시켰을 때는 相關係數 r=-0.865로서 各各 負의 相關關係를 보였다. 멸치 젓갈 熟成中의 DMA의 生成原因은 그 寄與率이 17℃일 때 r²≒0.66, 27℃일 때는 r²≒0.75로서 TMAO의 分解와 密接한 關連이 있는 것으로 判斷되었다. Dimethylamine(DMA) is known as an origin compound of dimethylnitrosamine which is responsible for carcinogenesis. It has been also reported that relatively large amount of DMA is distributed in fish muscle, particularly in salted and fermented fish. In this experiment, the degradation products of protein and trimethylaminoxide(TMAO) by the temperature conditions of 17℃ and 27℃ in the course of anchovy fermentation with 22% of salt were analysed, and the formation of DMA was discussed. Protein-N decreased through the whole formentation period in the conditions of 17℃ and 27℃ whereas amino-N increased proportionally to the decrease of protein-N, and the increasing rate of amino-N was remarkably faster at 27℃ than at 17℃. Trimethylamine(TMA) gradually increased with the decrease of TMAO till 69th day of fermentation, hereafter tended to slightly decrease. It seemed that the difference in fermentation temperature affects on the formation of DMA and obviously on the variation of TMAO. Both DMA and TMA content were inversely varied with the TMAO content. Correlation coefficient of DMA to TMAO in quantitative variation was shown -0.811 at 17℃ and -0.865 at 27℃ of fermentation temperature respectively. The results suggested that the formation of DMA during fermentation of anchovy was attributed to the degradation of TMAO showing contributorial ratio of 0.66 at 17℃ and 0.75 at 27℃ respectively.