http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
담수어육중의 타이아민, 라이보플라빈 및 나이아신 함량과 가열조건에 따른 변화
송영옥,조득문 부산대학교 가정대학 1993 家政大學硏究報告 Vol.19 No.-
The amounts of thiamin, riboflavin, and niacin in fresh water fishes live in Nak-Dong river were determined and the effects of heating conditions on change in the content of vitamins were also studied with carp meats. The amounts of vitamins were found to be varied a lot among different kinds fishes. The contents of thiamin and niacin in eel were the highest with 460mg% and 10.39mg%, respectively and goby showed the highest content in riboflavin with 3.55mg%. The amounts of riboflavin and niacin in carp were found to be the lowest and the thiamin in goby was the lowest among sample fishes. Vitamin B groups in eel were abundant compare to the others. The concentration of niacin and lipid content in fish were highly related. The linear regressions obtained from the thiamin content and either heating temperature or heating time were Y=-1.45X + 3.54 or Y=-5.51X + 0.02, respectively. The correlation coefficients of those were-0.96 and -0.97 which were statistically significant(p<0.01). Thiamin was readily destroyed by heat and the degree of destruction was much more dependent on the heating time than the heating temperature. When the effects of heating conditions on riboflavin and niacin were studied, destruction of these vitamins were depend only on the heating time, not on heating temperature. The change were statistically significant (p<0.05). It was found that the destruction of thiamin by heat was most serious among three vitamins.
혈합육어 Trypsin의 효소적 성질에 대한 반응속도론적 해석
조득문 ( Deuk Moon Cho ),허민수 ( Min Soo Heu ),김형락 ( Hyeung Rak Kim ),김두상 ( Doo Sang Kim ),변재형 ( Jae Hyeung Pyeun ) 한국수산학회 1996 한국수산과학회지 Vol.29 No.1
멸치, 고등어, 황다랭이 및 날개다랭이의 혈합육어에서 정제된 trypsin을 시료로 하여 각각의 BAPNA기질에 대한 반응속도와 그 관련 성질들을 분석 검토하였다. 4종의 혈합육어에서 정제된 trypsin의 Km`와 k(cat)는 멸치 trypsin이 각각 49.3μM과 90.9min 1, 고등어 trypsin A는 53.7μM과 61.2min 1 고등어 trypsin B는 96.5μM과 76.6min 1 황다랭이 trypsin은 62.8μM과 46.4min 1 그리고 날개다랭이 trypsin은 98.3μM과 47.68min 1이었다. TLCK에 대한 K1값은 멸치 trypsin이 20.90μM, 고등어 trypsin A가 2.86μM, 고등어 trypsin B가 3.90μM, 황다랭이 trypsin이 0.96μM, 그리고 날개다랭이 trypsin이 1.82μM이었으며, 황다랭이의 trypsin이 TLCK에 대하여 가장 예민하게 반응하였다. 이들 trypsin의 효소 활성과 촉매효율은 연근해 온 대산 혈합육어인 멸치와 고등어 trypsin이 열대해역에서 온대해역에 걸쳐 널리 회유하는 혈합육어인 황다랭이와 날개다랭이의 trypsin에 비하여 높은 특징을 보였다. Kinetic properties of trypsins purified from dark-fleshed fish (anchovy, mackerel, yellowfin tuna, and albacore) were examined and analyzed on benzoyl-(D,c)-arginine-p-nitroanilide (BAPNA). The values of Km` and k(cat) of the purified trypsins from the four dark-fleshed fish were found to be 49.3μM and 90.9min-1 for anchovy, 53.7μM and 61.2min-1 for mackerel A, 96.5μM and 76.6min-1 for mackerel B, 62.8μM and 46.6min-1 for yellowfin tuna, and 98.3μM and 47.7min-1 for albacore, respectively. The values of K, on tosyl-L-lysine chloromethyl ketone (TLCK) were determined to be 20.90μM for anchovy trypsin, 2.86μM for mackerel trypsin A, 3.90μM for mackerel trypsin B, 0.96μM for yellowfin tuna trypsin, and 1.82μM for albacore trypsin. Thus yellowfin tuna trypsin was the most sensitive to TLCK among all trypsins. The activities and catalytic efficiency of the trypsins purified from the temperate zone fish, anchovy and mackerel, were higher than those of the trypsins purified from yellowfin tuna and albacore which migrate widely from the tropic zone to the temperate zone.
혈합육어(멸치, 고등어, 황다랭이 및 날개다랭이)의 Trypsin - 2. 성질과 열 안정성
조득문(Deuk-Moon Cho),허민수(Min-Soo Heu),변재형(Jae-Hyeung Pyeun) 한국식품영양과학회 1993 한국식품영양과학회지 Vol.22 No.4
전보에 이어, 정제한 혈합육어 trypsin에 대하여 효소적 성질 및 열역학적 성질에 관하여 비교 검토한 내용을 요약하면 다음과 같다. 이들 혈합육어 trypsin은 BA-p-NA와 SP-p-NA 같은 amide기질 중 BA-p-BA기질만에 대하여, 그리고 ATEE, BAEE, BTEE 및 TAME 등의 ester기질 중에서는 BAEE와 TAME에 대하여만 현저한 활성을 보였다. 이들 효소는 antipain, leupeptin, DFT, TLCK, SBTI 등 화학약제와 금속이온 Cu^(2+) 및 Hg^(2+)에 의하여서는 그 활성이 현저히 저해를 받았으나, Mg^(2+)에 의하여서는 부활하였다. 이 효소들은 모두 50℃이상의 온도에서는 불안정하였으며, 날개다랭이의 trypsin이 온도 변화에 대하여 가장 안정하였다. 그리고, 활성화에너지는 멸치 trypsin이 13.91㎉/mole, 고등어 trypsin A는 11.61㎉/mole, 고등어 trypsin B는 8.43㎉/mole, 황다랭이 trypsin은 4.35㎉/mole, 그리고 날개다랭이 trypsin은 3.76㎉/mole이었다. In the present paper, enzymatic properties of the trypsins from the four dark fleshed fish were compared with each other and thermal stabilities of the enzymes were also investigated. The trypsins from the dark fleshed fish showed their activity only in BA-p-NA substrate of the amide substrates such as BA-p-NA and SP-p-NA, and BAEE and TAME of the ester substrates such as ATEE, BAEE, BTEE, and TAME. The enzymes were strongly inhibited by the serine protease inhibitors such as antipain, leupeptin, TlCK, DFP and SBTI, and were also inhibited by such metal ions as Cu^(2+) and Hg^(2+), but fairly activated by Mg^(2+). Denaturation constants of the enzymes were 13.4×10^(-4)sec^(-1) for anchovy trypsin, 47.18×10^(-4)sec^(-1) for mackerel trypsin A, 34.06×10^(-4)sec^(-1) for mackerel trypsin B, 42.28×10^(-4) sec^(-1) for yellowfin tuna trypsin and 16.6×10^(-4) sec^(-1) for albacore trypsin at 55°C. The activation energies of the trypsins at a temperature range of 30℃ to 50℃ were estimated to be 13.91㎉/mole for anchovy trypsin, 11.61㎉/mole and 8.43㎉/mole for mackerel trypsin A and for mackerel trypsin B, 4.35㎉/mole for yellowfin tuna trypsin, and 3.76㎉/mole for albacore trypsin.
Origin of the Multiple Type II Solar Radio Bursts Observed on December 31 2007
Cho, Kyung-Suk,Bong, Su-Chan,Kim, Yeon-Han,Kwon, Ryun-Young,Park, Geun-Seok,Moon, Yong-Jae,Park, Young-Deuk 한국우주과학회 2009 한국우주과학회보 Vol.18 No.2
Solar type II radio burst is regarded as a signature of coronal shock. However its association with coronal mass ejections (CMEs)-driven shock and/or flare blast waves remains controversial. On December 31 2007, SOHO/LASCO and STEREO/COR observed a CME th
Cho, Mi Young,Lee, Unn Hwa,Moon, Chang Hoon,Bang, Jong Deuk,Jee, Bo Young,Cha, Seung Ju,Kim, Jin Woo,Park, Myoung Ae,Do, Jeong Wan,Park, Jeong Woo Inter-Research 2012 Diseases of aquatic organisms Vol.101 No.2
<P>Two viral hemorrhagic septicemia virus (VHSV) isolates, VHSV-KR-CJA and VHSV-KR-YGH, were isolated from viral hemorrhagic septicemia disease outbreaks in flounder farms in South Korea. The VHSV-KR-CJA isolate was isolated from a flounder farm with high mortality (80%), while the VHSV-KR-YGH isolate was isolated from a flounder farm with low mortality (15%), suggesting that these isolates differ in virulence. The virulence of these isolates was evaluated in juvenile flounder via intraperitoneal injection. Consistent with their virulence in the field, mortality data revealed that the VHSV-KR-CJA isolate was highly pathogenic (cumulative mortality of 80%), while the VHSV-KR-YGH isolate was less pathogenic in flounder (cumulative mortality of 20%). To characterize the genotypes of these viruses, the full open reading frames (ORFs) encoding nucleoprotein N, phosphoprotein P, matrix protein M, glycoprotein G, nonstructural viral protein NV, and polymerase L of these viruses were sequenced and analyzed. Sequence analysis revealed that both isolates are genetically very similar (identical amino acid sequences for P, M, NV, and L and >99.7 and 99.8% amino acid sequence identity for N and G, respectively). Phylogenetic analysis indicated that both of these viruses belong to the Genotype IVa group, suggesting that they originated from a common ancestral virus. The low pathogenicity VHSV strain may potentially evolve to become a more pathogenic strain through only a few nucleotide substitutions. Further functional analyses of mutations in VHSV genes are necessary to identify factors that determine VHSV pathogenicity in flounder.</P>