• Journal of the Korean Society of Clothing and Textiles
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• v.22 no.7
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• pp.843-850
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• 1998

The purpose of this study is the investigation of chemical properties of wool treated with oxidants and protease at low temperature. The chemical degradation of the fibers were investigated by measuring $\alpha$-amimo acid contents and FT-IR analysis. In addition, urea-hydrogensulfite solubility was measured to compare to the oxidation and protease treated wool. The results were as follows. 1) By the oxidation of wool, cystine is oxidised to cysteic acid by way of the intermediate oxides, cystine-S-monooxide and cystine-S-dioxide, in the case hydrolysis catalysed by the protease catalyse. Also, $\alpha$-amimo acid contents is increased, and urea-hydrogensulfite solubility was lower than that of untreated wool. This chemical degradation of wool was occurred due to oxidate hydrolysis in the order of permonosulfate>dichloroisocyanuric acid$\geq$chlorine. 2) The chemical degradation of wool was accelerated by the protease treatment of oxidized wool. Oxidation of wool is considered to make the fiber more susceptibled to enzymatic attact by opening disulphide bond within wool. Enzymatic attact was effectively directed to the wool oxidised by permonosulfate.

• BMB Reports
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• v.28 no.2
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• pp.87-93
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• 1995

To investigate the biological functions of the EGF-like domain of mouse betacellulin (BTC), mouse BTC(33-80), a 48-residue peptide corresponding to the EGF-like domain, was synthesized by stepwise solidphase methods using a 9-fluorenylmethoxycarbonyl (Fmoc) strategy. The homogeneity of synthetic mouse BTC(33-80) was confirmed by analytical reversed phase (RP)-HPLC, amimo acid analysis, and fast atom bombardment mass spectrometer (FAB-MS). Three disulfide bond pairings of synthetic mouse BTC(33-80) were established by amino acid analysis of cysteine-containing fragments derived from thermolytic digestion. These were consistent with the pairings of EGF and transforming growth factor ($TGF-{\alpha}$). The EGF-Iike domain of mouse BTC showed equipotent activity in both EGF-receptor binding on A-431 epidermoid carcinoma cells, and mitogenesis on NIH-3T3 fibroblast cells, as compared with authentic h-EGF. Results suggest that the EGF-Iike domain of BTC plays a significant role in mitogenic activity with an EGF-receptor mediated system.

• The Korean Journal of Food And Nutrition
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• v.19 no.1
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• pp.8-13
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• 2006

This study was designed to investigate the physicochemical properties of the Sargassum thunbergii, by measuring general composition, minerals, amino acid, free sugar, peroxide value(POV) and thiobarbituric acid reactive substances(TBARS). The contents of crude protein and crude lipid in Sargassum thunbergii were $15.7{\pm}0.8%\;and\;0.9{\pm}0.4%$, respectively. Total content of amino acids was 5,635.5 mg/100 g. The glutamic aid($1,071.3{\pm}1.8mg/100g$) content was the highest, followed by aspartic acid($645.9{\pm}1.4mg/100g$) and phenylalaine ($470.1{\pm}1.4mg/100g$). Galactose and mannose of all free sugar showed the highest values $40.2{\pm}0.5mg/100g\;and\;22.3{\pm}0.4mg/100g$. All solvent extracts of Sargassum thunbergii showed lower POV than ascorbic acid, and chloroform extracts showed the strongest antioxidant activity(4.0 meq/kg) at 12 hours storage. TBARS of chloroform extract were 2.8 mg MDA/L in $FeCl_2$ and 0.9 mg MDA/L in $CuSO_4$ oxygen species.