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Cho, Eun-Wie,Park, Jung-Hyun,Na, Shin-Young,Kim, Kil-Lyong Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.5
Biotinylation of recombinant proteins is a powerful tool for the detection and analysis of proteins of interest in a large variety of assay systems. The recent development of in vivo biotinylation techniques in E. coli has opened new possibilities for the production of site-specifically biotinylated proteins without the need for further manipulation after the isolation of the recombinantly expressed proteins. In the present study, a novel vector set was generated which allows the convenient cloning and expression of proteins of interest fused with an N-terminal in vivo biotinylated thioredoxin (TRX) protein. These vectors were derived from the previously reported pBIOTRX vector into which was incorporated part of the pBluescript II+phagemid multiple cloning site (MCS), amplified by PCR using a pair of sophisticated oligonucleotide primers. The functionality of these novel vectors was examined in this system by recombinant expression of rat transforming growth factor-$\beta$. Western-blot analysis using TRX-specific antibodies or peroxidase-conjugated streptavidin confirmed the successful induction of the fusion protein and the in vivo conjugation of biotin molecules, respectively. The convenience of molecular subcloning provided by the MCS and the effective in vivo biotinylation of proteins of interest makes this novel vector set an interesting alternative for the production of biotinylated proteins.
Cho, San-Soon,Lee, Hyo-Ku,Han, Chi-Won,Seong, Eun-Soo,Yu, Chang-Yeon,Kim, Myong-Jo,Kim, Na-Young,Kang, Wie-Soo,Ko, Sang-Hoon,Son, Eun-Hwa,Choung, Myoung-Gun,Lim, Jung-Dae The Korean Society of Food Science and Nutrition 2008 Preventive Nutrition and Food Science Vol.13 No.3
Fish protein hydrolysates (FPHs) with different degrees of hydrolysis by treatment with alcalase, pronase, flavourzyme and trypsin and isolated peptide were prepared from Hwangtae (yellow dried pollack, Theragra chalcogramma). Hwangtae protein hydrolysate was fractionated according to the molecular weight into six major types of APO1 (1.3 kDa), APO2 (1 kDa), APO3 (<1 kDa), APACE (<1 kDa), APG1 (70 kDa) and APG2 (70 kDa) isolated from the hydrolysate using consecutive chromatographic methods. Soluble peptide were produced from Hwangtae and evaluated for their nutritional and functional properties. Some functional properties of FPHs were assessed and compared with those of egg albumin or the soybean protein. APO2 had the highest nitrogen solubility value (94.2%), emulsion capacity and emulsion stability of the Alaska Pollack peptide ranged from 12.4 to 39.5 (mL of oil per 200 mg of protein) and 44.0% to 77.5%, respectively. Highest and lowest fat adsorption values were observed for APG1 (9.9 mL of oil per gram of protein) and APO3 (3.8 mL of oil per gram of protein), respectively.
San Soon Cho,Hyo Ku Lee,Chi Won Han,Eun Soo Seong,Chang Yeon Yu,Myong Jo Kim,Na Young Kim,Wie Soo Kang,Sang Hoon Ko,Eun Hwa Son,Myoung Gun Choung,Jung Dae Lim 한국식품영양과학회 2008 Preventive Nutrition and Food Science Vol.13 No.3
Fish protein hydrolysates (FPHs) with different degrees of hydrolysis by treatment with alcalase, pronase, flavourzyme and trypsin and isolated peptide were prepared from Hwangtae (yellow dried pollack, Theragra chalcogramma). Hwangtae protein hydrolysate was fractionated according to the molecular weight into six major types of APO1 (1.3 kDa), APO2 (1 kDa), APO3 (<1 kDa), APACE (<1 kDa), APG1 (70 kDa) and APG2 (70 kDa) isolated from the hydrolysate using consecutive chromatographic methods. Soluble peptide were produced from Hwangtae and evaluated for their nutritional and functional properties. Some functional properties of FPHs were assessed and compared with those of egg albumin or the soybean protein. APO2 had the highest nitrogen solubility value (94.2%), emulsion capacity and emulsion stability of the Alaska Pollack peptide ranged from 12.4 to 39.5 (mL of oil per 200 mg of protein) and 44.0% to 77.5%, respectively. Highest and lowest fat adsorption values were observed for APG1 (9.9 mL of oil per gram of protein) and APO3 (3.8 mL of oil per gram of protein), respectively.