• Journal of Ginseng Research
• /
• v.13 no.2
• /
• pp.254-259
• /
• 1989

A radioprotective ginseng protein fraction was obtained from Korean white ginseng powder by the following isolation and purification procedures: Tris-HCI buffer extraction, 70% ammonium sulfate fractionation, CM-rellulosr column chromatography, heat inactivation and Sephadex G-75 column chromatography. This fraction was further purified by Sepharose 4B and Sephadex G-150 column chromatographies. Three fractions obtained were subjected to Native-PAGE and SDS-PAGE using gradient gels and the silver staining method. Molecular weights of the native proteins and their subunits were estimated.

• YAKHAK HOEJI
• /
• v.41 no.5
• /
• pp.638-646
• /
• 1997

The steroid 9${alpha}$-hydroxylase activity has been detected in cytosol fraction, $100,00{\times}g$ supernatant of cell free extract of Mycobacterium fortuitum. The activity was not linear with protein concentration in the assay suggesting 9${alpha}$-hydroxylase is a multicomponent enzyme. The 9${alpha}$-hydroxylase system was partially purified through fractional saturation of ammonium sulfate, strong anion exchange (Mono Q) column chromatography, gel filtration (Superose 12) column chromatography, and testosterone affinity gel chromatography. Ammonium sulfate 50~60% saturated fraction of the cytosol gave 9${alpha}$-hydroxylase activity. For further purification, the half-saturated ammonium sulfate fraction was applied to Mono Q, Superose 12, or affinity gel column. The purification factors of 9${alpha}$-hydroxylase containing fraction after Mono Q, Superose 12, and affinity gel chromatography was 13, 11, and 17 respectively.

• Korean Journal of Food Science and Technology
• /
• v.16 no.4
• /
• pp.472-474
• /
• 1984

Gel filtration of water soluble protein of soybean and cotyledon of sprout at various growth stages by using Sephadex G-200 showed 5 fractions (A,B,C,D and E). According to gel filteration and disc gel electrophoresis, fraction B,C and D were identified as 11S,7S and 2S, respectively. Fraction A was turbid substance and fraction E showed 1 peak. During growth of sprout 7S decreased firstly, 2S secondly and 11S lastly in cotyledon. Fraction A increased until 6th day and decreased thereafter while E increased throughout the growth. In axis only two fractions (11S+7S and E) were showed, and 11S+7S fraction was little changed and fraction E increased slightly with the growth.

• Applied Biological Chemistry
• /
• v.30 no.1
• /
• pp.88-94
• /
• 1987

To investigate ginseng oligopeptides with biological activities, the water extract was purified by ultra-filtration, gel filtration, ion-exchange and thin layer chromatography. Ultra-filtered water extract exhibited antilipolytic activity, inhibiting epinephrine-induced lipolysis in the isolated fat cells of rat epididymal adipose tissue. The filtrate was separated into 3 fractions by Sephadex G-25 gel filtration. Peptides were found only in the first fraction(S-FI). Saponine and sugars were also detected in tie fraction. S-FI fraction resolved further into 6 fractions by Dowex 50 ion-exchange chromatography. The sugar and saponine depleted fraction(P-F2) from the second chromatography showed antilipolytic activity. The P-F2 fraction revealed 6 spots on TLC. The 6 spots were isolated by TLC and identified as peptides.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.17 no.1
• /
• pp.13-17
• /
• 1988

$HF_1$(1H KOH soluble hemicellulose fraction), $HF_2$(2H KOH soluble hemicellulose fraction) $HF_3$(3H KOH soluble hemicellulose fraction) and $HF_4$(4H KOH soluble hemicellulose fraction) were fractionated from Fuji crude cell wall and purified using Sephacryl S-500 to determine the effects of these hemicellulosic fractions on the Ca- pectate gel formation. By increasing of KOH concentration, from 1 to 4N, hexose peas became higher in led, and molecula weights, especially pentose peaks in high molecular weight. Hemicellulose fractions using gel filtration were composed of $8{\sim}10$ peaks which were $10^4{\sim}143{\times}10^4$ molecular weight. Higher values of hardness, adhesiveness and gumminess were found in low molecular weight than in high molecular weight, also in hexose and uronic acid contained than in hexose contained.

• Korean Journal of Agricultural Science
• /
• v.22 no.1
• /
• pp.82-95
• /
• 1995

These experiments were carried out to isolate SIgA from human and bovine milk. The immunochemical properties of SIgA from human and bovine milk were examined by Gel filtration, DEAE and SDS-PAGE. Double Immunodiffusion, and Immunoelectrophoresis. The results obtained are as follows: 1. Human SIgA was purified from colostrum of Korean women by repeated gel filtration on Sephadex G-200 and Sepharose 6B, but bovine SigA was not cleary purified from bovine colostrum of Holstein cows by anion exchange chromatography using DEAE-Sephadex A-50 and gel filtration on Sephadex G-200 and Sepharose 6B. 2. The immunochemical properties of fractions from gel filtration on the Sephadex G-200 and Sepharose 6B column as assessed by Immunoelectrophoresis and double Immunodiffusion to identify the presence of IgM in first peak fraction, and the presence of pure SIgA in second peak fraction. However, Bovine SigA rich fraction from bovine colostrum of Holstein cows contained a large amount of $IgG_1$-dimer in addition to SIgA. 3. The fragments of reduced bovine colostrum SIgA rich fraction were estimated to have molecular weights of secretory component, heavy chain and light chain (75,000-80,000, 50,000-60,000, 25,000-27,000 daltons) by SDS-PAGE, respectively. Those were similar to the molecular weight of reduced SIgA from human milk.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.41 no.3
• /
• pp.176-181
• /
• 2008

To evaluate the effective use of endoprotease from squid viscera as a food processing aid, various methods of fractionating endoprotease from viscera of the Argentina shortfin squid (Illex argentinus) were evaluated. The endoprotease-positive fractions of each fractionation were fraction II (30-40%, w/w) with cold acetone, fraction IV (50-60% saturation) with ammonium sulfate, fraction UF with anion exchange chromatography, and fraction II (15-24 kDa) with gel filtration. The specific activities (approximately 25 U/mg) of the fractions using ammonium sulfate and gel filtration were higher than the others. Total azocaseinolytic activity and recovery of the positive fraction using gel filtration were 806.95U and 37.82%, respectively, and were the highest among the positive fractions. Based on the results, gel filtration was the most efficient method for fractionating endoprotease from the viscera of Illex argentinus.

• Journal of Animal Science and Technology
• /
• v.47 no.6
• /
• pp.1025-1032
• /
• 2005

This study was carried out to separate ovotransferrin in chicken egg white by gel chromatography and heparin affinity chromatography. In gel filtration which was performed with 50mM Phosphate buffer (pH 7.2, 0.15M salt) at a flow rate of 2.0 ml/min, ovotransferrin and ovalbumin were eluted together in fraction number 11-16. In order to separate pure ovotransferrin, fraction No. 12-14 of them which have high concentration of ovotransferrin were concentrated and rechromatographed. However, the ovotransferrin did not separated clearly. In heparin affinity chromatography, the separation was performed with 50mM ethylaminetetraacetic acid (EDTA, pH7.2) and 50mM Phosphate buffer (pH 7.2, 0.15M salt contained) on ferrous and ferric ion saturated column at as same flow rate as gel filtration system's. Ovotransferrin and albumin were eluted together at 10-15min (fraction No.3) and 15-20min (fraction No.4), respectively. However, purified ovotransferrin was eluted at 156-165min and 165-175min (tube No.32-33) with 50 mM phosphate buffer (pH 7.2, 0.15M salt free), respectively. Heparin affinity chromatography with ferric ion saturated column was resulted in the best separation of ovotransferrin rather than separation by gel chromatography and ferrous ion saturated heparin affinity chromatography.

• The Korean Journal of Pesticide Science
• /
• v.14 no.4
• /
• pp.347-360
• /
• 2010

In order to develop the multi-residue purification method for 180 pesticides commonly used in Korea, many analytical methods on individual and multi- pesticide residues in the agricultural commodities and food product were examined. Through the modification of adsorption chromatographic methods used in Europe, the United States and Korea, the Florisil and silica-gel chromatographic systems were developed. Through these purification systems, elution profiles for all pesticides were examined. As the results, 145 pesticides were recovered in the range of 70-120% in Florisil clean-up system. The distribution of pesticides in the elution profile was 12 pesticides in the first fraction, 76 pesticides in the second fraction, 81 pesticides in the third fraction, 60 pesticides in the fourth fraction and 30 pesticides in the last fraction. And, in silica-gel system, 137 pesticides were recovered in the range of 70~120%. The distribution of pesticides in the elution profile was 22 pesticides in the first fraction, 59 pesticides in the second fraction, 102 pesticides in the third fraction, 46 pesticides in the fourth fraction and 8 pesticides in the last fraction.

• Fisheries and Aquatic Sciences
• /
• v.17 no.2
• /
• pp.181-187
• /
• 2014

This study was performed to identify the optimum fractionation method and conditions to obtain exopeptidase-active fractions from octopus hepatopancreas (HP) crude extracts (CEs) using four techniques: solid ammonium sulfate fractionation, polyethylene glycol (PEG) fractionation, anion exchange chromatography, and gel filtration chromatography. The fractions with the highest total activity toward L-leucine-p-nitroanilide (Leu-pNA) were fraction IV from the ammonium sulfate and PEG fractionation, and fraction II in ion exchange and gel filtration chromatography. The total exoprotease activity of these fractions was highest in fraction IV (4,050.20 U) of ammonium sulfate fractionation, followed by fraction II (3,600.28 U) from gel filtration chromatography, fraction IV (2,861.30 U) from PEG fractionation, and fraction II (2,576.28 U) from ion exchange chromatography. These results suggest that ammonium sulfate fractionation using 60-80% ammonium sulfate was the most efficient method for separating the exoprotease active fractions from CEs of octopus HP.