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Yang, Jeng-Huh,Lin, Chin-Wen Asian Australasian Association of Animal Productio 2000 Animal Bioscience Vol.13 No.12
Extended use of porcine blood in food ingredients depends on the decolorization of red blood cell concentrates and the modification of its functional properties. The purpose of this study is to compare the relative effect of cation ion exchanger for decolorization of porcine red blood globin. The globin extract is freeze-dried for determination of various functional properties, such as solubility, emulsion capability and foaming ability. Since the isoelectric point of blood globin is located at pH 6.8, which is the neutral pH ranges (6-8), so its functionalities are inferior around these pHs. This weakness has been the main reason, which limit the extended use of blood globin in food industry. Acetylation and succinylation of blood globin can be an alternative way to improve its functionalities. These results may provide new information to understand the decolorization mode by cation ion exchanger for the blood globin. With chemical, the functionalities of blood globin could be obviously improved. The above findings could enable food industry to extend the use of blood globin as a food ingredient.
Huh, Tae Lin,PARK, HEE SUNG,Jeng, Jiingjau,Kim, Young Ou,Oh, II Ung,Song, Byoung J. 경북대학교 유전공학연구소 1995 遺傳工學硏究所報 Vol.10 No.1
A 0.6 kb cDNA fragment encoding the human NAD^+-specific isocitrate dehydrogenase α-subunit (H-IDHα) was amplified by PCR using oligonucleotide primers synthesized on the basis of pig tryptic peptide sequences [Huang and Colman (1990) Biochemistry 29, 8266-8273]. With the amplified cDNA as a probe, cDNA clones for IDHα were isolated from a human heart λgt11 cDNA library. The deduced protein sequence of the largest cDNA clone (2628 bp) rendered a precursor protein of 366 amino acids (39591 Da) and a mature protein of 339 amino acids (36640 Da). The deduced H-IDHα protein sequence is highly similar to the partial peptide sequences of the pig enzyme. It is 55, 43 and 44 % identical with yeast NAD^+-specific IDH2, yeast NAD^+-specific IDH1 and monkey NAD^+-specific IDH γ-subunit (IDHγ) respectively. However, it has less similarity (about 30%) to NADP^+-specific IDH from Escherichia coli and bovine mitochondria. These results indicate that the structure of IDHα closely resembles that of IDH2, the catalytic subunit of the yeast enzyme. Structural analysis of the deduced H-IDHα protein revealed that the amino acids responsible for the binding of isocitrate, Mg^(2+) and NAD^+ are highly conserved. It also has two conserved motifs for the binding sites of ATP and ADP, but a canonical Ca^(2+)-binding motif was not recognized. Unusual penta- (ATTTA) and tri-(TAA or ATT) nucleotides which are respectively believed to interact with RNA-binding proteins and be near the endonuclease cleavage sites were frequently recognized in its 3' untranslated region, indicating the possibility of an additional method of regulation of this enzyme. Northern-blot analysis suggests that one mRNA transcript (2.8 kb) exists in cultured HeLa cells. Genomic DNA Southern-blot analysis indicates that the IDHα gene is not closely related to that of the other IDH isoenzymes, and IDHα appears to be encoded by a single gene.
Lin, Chin-Wen,Yang, Jeng-Huh,Chu, Hsien-Pin,Su, Ho-Ping,Chen, Hsiao-Ling,Huang, Chia-Cheong Asian Australasian Association of Animal Productio 2001 Animal Bioscience Vol.14 No.3
The physiochemical properties and interactions between porcine blood and waxy rice were determined. Addition of calcium chloride (0.15%) improved acceptability of blood cake and increased the gelatinization degree of waxy rice. The water-holding capacity of porcine blood gel (blood/water=60/40, v/v), extent of absorption and gelatinization of waxy rice, and scanning electron microscopy showed that blood protein matrix and waxy rice are competitors for holding water in the cooking procedure. Non-haem iron content increased linearly (R=0.95) when heating temperature rose. The presence of blood proteins caused increasing of peak temperature (Tp) of gelatinization in differential scanning calorimetric thermal gram, The microstnlcture of plasma proteins and haemoglobin appeared continuous changes, and interacted with surface of waxy rice flour in terms of network and mosaic form, respectively. The electrophoretic patterns revealed an interaction between plasma proteins and waxy rice glutelin and haemoglobin when heated could be found at temperatures above $60^{\circ}C$.
Study on a Binder by Using Porcine Blood Plasma Transglutaminase, Thrombin and Fibrinogen
Tsai, Chong-Ming,Tseng, Tsai-Fuh,Yang, Jeng-Huh,Chen, Ming-Tsao Asian Australasian Association of Animal Productio 2006 Animal Bioscience Vol.19 No.1
The purpose of this study was to prepare a binder containing porcine blood transglutaminase (TGase), thrombin and fibrinogen. Extracted TGase, thrombin and fibrinogen were used alone or mixed with different proportions of their volume (v/v/v) by nine combinations as follows were 0.5:1:15, 0.5:1:20, 0.5:1:25, 1:1:15, 1:1:20, 1:1:25, 1.5:1:15, 1.5:1:20 and 1.5:1:25, respectively. Five ml of each combination were mixed with 0.6 ml of 0.25 M calcium chloride before experiment. After storage at 4C for 0, 1, 2, 3, 4 and 5 weeks, enzyme activity, total plate count, pH value, and SDS-PAGE of TGase, thrombin and fibrinogen were tested and pH value, clotting time and gel strength of the nine combination binders were determined. The results showed that total plate count of thrombin and pH value of TGase were significantly higher (p<0.05) than in other treatments. SDS-PAGE results showed that purified TGase, thrombin and fibrinogen from porcine blood plasma compared with commercial products (Sigma) had the same band patterns and nine different combination binders had no significant effect. Enzymatic activity of TGase and thrombin decreased as storage time increased. Total plate count of TGase, thrombin and fibrinogen and clotting time of the binder increased as storage time increased. The higher amount of fibrinogen in combinations, the stronger the gel strength.
Tseng, Tsai-Fuh,Tsai, Chong-Ming,Yang, Jeng-Huh,Chen, Ming-Tsao Asian Australasian Association of Animal Productio 2006 Animal Bioscience Vol.19 No.7
The purpose of this study was to use pig blood plasma transglutaminase (TGase) combined with thrombin and fibrinogen as a binder, which was applied to restructured meat, and to investigate its effect on the restructured meat quality. Pig meat was obtained 10 h post mortem from a traditional market was ground using a 10 mm aperture plate. A binder admixture was added (TGase:thrombin:fibrinogen mixed as 0.5:1:20 (v/v/v) to which was added 12% of its volume of 0.25 M calcium chloride) at 0, 5, 10, 15 and 20% of meat weight. Measurements included cooking loss, shrinkage rate, shear value, total plate count, pH value, TBA value, color difference, tension strength and sensory evaluation. The results showed that ground meat containing 20% w/w of binder admixture had higher cooking loss, shrinkage rate and shear value (p<0.05). Addition of different percentages of binder admixture did not affect total plate count, pH value, TBA value, and sensory evaluation of restructured meat (p>0.05). Tension strength was increased with increased level of binder admixture. Addition up to 15% binder admixture to restructured meat showed better scores of sensory texture, flavor and total acceptability (p<0.05).
KIM, SUNG MIN F,Kim, Byung Moon,Jeng, Jiingjau,Soh, Yun jo,Bak, Choong Il,Huh, Jae Wook,Song, Byoung J 생화학분자생물학회 1980 BMB Reports Vol.29 No.2
A 2.1 kb cDNA clone for rat transketolase was isolated from rat liver λgt11 cDNA library and its sequence was determined. The predicted rat transketolase (655 amino acids with M_r 71,186) is highly similar (92%) to that of the human enzyme except that it contains an extra 32 amino acids at its N-terminus. Although it is less similar ($lt;27%) to transketolases from non-mammalian species, the functional motifs such as the catalytic sites and thiamine binding domain are well conserved in the rat enzyme. Southern blot analysis of genomic DNA verified that transketolase appears to be derived from a single gene. Immunoblot and Northern blot analyses suggested that hepatic transketolase was activated pretranslationally by a 2.1fold while little change was observed in brain enzyme, indicating a tissue-specific pretranslational activation during postnatal development.
Kim, Sung-Min F.,Kim, Byung-Moon,Jeng, Jingjau,Soh, Yun-Jo,Bak, Choong-Il,Huh, Jae-Wook,Song, Byoung-J. Korean Society for Biochemistry and Molecular Biol 1996 Journal of biochemistry and molecular biology Vol.29 No.2
A 2.1 kb cDNA clone for rat transketolase was isolated from rat liver ${\lambda}gt11$ cDNA library and its sequence was determined. The predicted rat transketolase (655 amino acids with $M_r$ 71,186) is highly similar (92%) to that of the human enzyme except that it contains an extra 32 amino acids at its N-terminus. Although it is less similar (<27%) to transketolases from non-mammalian species, the functional motifs such as the catalytic sites and thiamine binding domain are well conserved in the rat enzyme. Southern blot analysis of genomic DNA verified that transketolase appears to be derived from a single gene. Immunoblot and Northern blot analyses suggested that hepatic transketolase was activated pretranslationally by a 2.1-fold while little change was observed in brain enzyme, indicating a tissue-specific pretranslational activation during postnatal development.
윤달환(Dal-Hwan Yoon),배동주(Dong-Joo Bae),김형묵(Hyung-Mook Kim),권오훈(Oh-Hoon Kwon),고영현(Young-Hyun Ko),허정화(Jeng-Hwa Huh),김호균(Ho-Keun Kim) 대한전기학회 2006 대한전기학회 학술대회 논문집 Vol.2006 No.10
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