• Proceedings of the Ginseng society Conference
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• 1980.09a
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• pp.53-57
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• 1980

Red ginseng powder was administered at a dose of 2.7 g per day for 3 months to 21 diabetic patients who were under the treatment with insulin. It was found that the ginseng powder was effective to 12 patients and ineffective to 9 patients. Based on these clinical results, experiments were carried out to elucidate factors which concerned with improvement of pathological conditions of diabetes mellitus. In the previous symposium, we reported that red ginseng powder contained an anti-lipolytic peptide, or an insulin-like peptide. In the course of purification of the insulin-like peptide in the ginseng, we found another fraction which possessed anti-lipolytic activity. The anti-lipolytic factor of the fraction was purified by gel filtration on Bio Gel P-2 column and Dowex $50W{\times}4$ column chromatography. The character of the finally purified material was examined by thin-layer chromatography, high-speed liquid chromatography and mass spectrometry. With these examinations, the active principle was indentified to be adenosine. Pharmacological significance of these insulin-like substances, the peptide and adenosine, was discussed.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.76-76
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• 2003

Here we report an antifungal peptide isolation from G. mellonella larvae. The peptide shows a high degree of sequence homology to an insect defensin, named heliomicin, first reported in Lepidoptera. The peptide was purified by a three-step procedure consisting of acid extraction, gel permeation chromatography and reversed-phase HPLC. First the N-terminal amino acid sequence of the purified peptide was determined by automated Edman degradation. (omitted)

• Korean Journal of Plant Resources
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• v.20 no.6
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• pp.518-523
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• 2007

Lunasin is small subunit peptide of coded from Gm2S-1 gene in soybean. It has been previously demonstrated that lunasin is a novel and promising cancer preventive peptide. Lunasin peptide is found only in the seed and not other tissues. And lunasin peptide starts to appear at 5 weeks after flowering and remains in the mature seed. We report here firstly lunasin peptide identified from soybean callus induced by the tissue culture and demonstrate its anticancer properties. The lunasin was identified and purified from soybean callus aged for 6 months. The callus lunasin($1{\mu}M$) inhibited the acetylation of histone H3 and H4 by 58.8% and 56.5%, respectively. And it fully inhibited foci formation compared to the values of the positive control(no lunasin) and negative control(no MCA). Purified lunasin was able to internalize into the cell and localized in the nucleus.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.3
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• pp.466-472
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• 1997

Peptides separated from fish paste washing liquid of an Alaska pollak (Theragria chalcogramma) were purified and characterized. The fish paste washing liquid (supernatant) was separated by centrifugation of fish paste homogenate. The fish paste washing liquid of $0.5\%$ concentration was hydrolyzed for 24 hour at $50^{\circ}C$ by immobilized protease in bioreactor and decomposing liquid of protein having $50\%$ decomposing rate (OPA method) was obtained. The crude peptide fractions were obtained from this liquid by Dowex 50w $(H^+)$ column chromatograpy. Purified peptides (SP-fraction peptides) were fractionated by using SP-Sepadex C-25 $(H^+)$ column chromatography. Molecular weights and amino acid compositions of these peptides were estimated by Sephadex G-50 column chromatography and HPLC, respectively. when the washed peptides was eluated with $0.6\~0.9\%\;and\;1.2\~2.0\%$ of NaCl, peptides composed of weakly basic amino acids and strongly basic amino acid were respectively eluted. Molecular weights of each peptide fractions showed the broad distribution from 1,000 Da to 3,000 Da in the order of SP-4>SP-3>SP-2>SP-1. Peptides contained a large quantity of glycine, arginine, glutamic acid, and alanine in the washed peptide and its SP-tractions, respectively.

• Applied Biological Chemistry
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• v.41 no.4
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• pp.270-272
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• 1998

Angiotensin converting enzyme (ACE) inhibitor was isolated from beef bone extract hydrolysate. After hydrolysis of beef bone extract with a commercial protease, ACE inhibitory peptide was purified by using ultrafiltration, gel permeation chromatography, and reverse-phase high pressure liquid chromatography. The purified ACE inhibitor was a pentapeptide, Gly-Pro-X-Gly-Pro.

• Journal of Life Science
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• v.26 no.3
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• pp.296-301
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• 2016

An antibacterial peptide from skin extract of the catfish Silurus asotus was purified and characterized. The acidified skin extract was put through a Sep-Pak C18 solid phase extraction cartridge using a stepwise gradient and divided into flow-through (F.T.), 10% methanol-elute (RM10), 60% methanolelute (RM60), and 100% methanol-elute (RM100) fractions. RM10, RM60, and RM 100 showed antimicrobial activity against Escherichia coli D31. On the other hand, the F.T. fraction did not show antimicrobial activity. Among the various fractions, RM 60 had the highest activity. RM 60 was partially purified on a cation exchange column (CM52) by a stepwise gradient. The ammonium acetate (pH 5.15) 0.02 M – 0.8 M fraction showed antimicrobial activity. Then an antimicrobial peptide was purified using a 0.6M fraction with strong antibacterial activity through a series of five C18 reversed-phase HPLC columns. For the characterization of the purified peptide, the molecular weight and amino acid sequence were analyzed by MALDI-TOF MS and Edman degradation. The molecular weight of this peptide was about 4182.1 [M+H]⁺. The amino acid sequence of this peptide was partially determined as follows: PALXXKARREAKVKF. These findings suggest that this peptide plays a significant role in the innate defense system of catfish skin.

• YAKHAK HOEJI
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• v.47 no.3
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• pp.184-189
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• 2003

Peptide deformylase (PDF) is essential and unique to bacteria, thus making it an attractive target for the discovery of novel antibacterial drugs. PDF deformylates the N-formylmethionine of newly synthesized polypeptides in prokaryotes. In this study, a pdf gene from Staphylococcus aureus 6538p was cloned in pET-14b vector and PDF protein was over-produced in Escherichia coli BL21 (DE3). NH$_2$-terminal His-tagged PDF protein was purified by nickel-nitrilotriacetic acid (Ni-NTA) metal-affinity chromatography. Enzymatic activity of purified 6xHis-tagged PDF was tested on the substrate (formyl-Methionine-Alanine-Serine) by formate dehydrogenase-coupled spectrometric assay of peptide deformylase. For the discovery of new PDF inhibitors from chemical libraries and culture broths of soil bacteria, a target-oriented screening system using a 96-well plate was developed. About 3,000 commercial chemical libraries were tested in this screening system, and 2 chemicals (0.07％) among them showed an inhibitory activity against PDF enzyme. This result showed that a new screening system can be used for the discovery of new PDF inhibitors.

• Fisheries and Aquatic Sciences
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• v.24 no.4
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• pp.163-170
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• 2021

Peptides are naturally occurring biological molecules that are found in all living organisms. These biologically active peptides play a key role in various biological processes. The aim of this study is the extraction and the purification of bioactive materials that induce relaxation of an apical muscle from the pyloric caeca of Patiria pectinifera. The acidified pyloric caeca extract was partially separated by the solid phase extraction using a stepwise gradient on Sep-Pak C18 cartridge. Among the fractions, materials eluted with 60% methanol/0.1% trifluoroacetic acid was put a thorough of a series of high performance liquid chromatography (HPLC) steps to isolate a neuropeptide with relaxation activity. The purified compound was eluted at 28% acetonitrile in 0.1% trifluoroacetic acid with retention time of 25.8 min on the CAPCELL-PAK C18 reversed-phase column. To determine the molecular weight and the amino acid sequence of the purified peptide, LC-MS and Edman degradation method were used, respectively. The primary structure of the peptide was determined to be FGMGGAYDPLSAGFTD which corresponded to the amino acid sequence of a starfish myorelaxant peptide (SMP) isotype (SMPb) found in the cDNA sequence encoding SMPa and its isotypes. In this study, a muscle relaxant neuropeptide (SMPb) has been isolated from pyloric caeca of starfish P. pectinifera. This is the first report of SMPb isolation on the protein level from P. pectinifera.

• Food Science of Animal Resources
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• v.43 no.1
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• pp.10-24
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• 2023

In this study, a antioxidant activity peptide fraction was separated and purified from metabolites of whey protein fermented by Lactobacillus rhamnosus B2-1. The fermentation sample was separated by macroporous resin D101 and Sephadex G-15. The collected fractions were tested for antioxidant and antitumor activities. In order to test the antioxidant activity of fractions, Hydroxyl (·OH), 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid (ABTS), and Oxygen Radical Absorbance Capacity (ORAC) were used. The final purified peptide B11 showed highest ABTS and ·OH radical scavenging rate by 84.36±1.89% and 62.43±2.64%, respectively, and had an ORAC activity of 1,726.44±2.76 μM Trolox equivalent/g. Further, the inhibitory effect of B11 on the proliferation of LoVo human colon cancer cells, KB and Cal-27 human oral cancer cells were enhanced with increasing concentrations of B11. B11 contains 51.421% amino acids, with Glu and Asp being the major constituents. In this study, we obtained peptide fraction B11 with antioxidant activity, which is promising for development.

• Biomolecules & Therapeutics
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• v.2 no.4
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• pp.303-309
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• 1994

The analysis of membrane receptors for hormones and neurotransmitters has progressed considerably by pharmacological and biochemical means and more recently through the use of specific antibodies. Two kinds of antibodies could be produced, one is from synthetic peptides and the other from proteins such as purified receptor. Anti-peptide antibodies gave some advantages; epitope is evident and also receptor purification in quantity is not prerequisite. It can be also applied to the study of receptor structure-activity relationship. The purpose of the present study was 1) to produce and characterize a polyclonal antibody against a synthetic $\beta$2-adrenergic receptor peptide(Phe-Gly-Asn-Phe-Trp-Cys-Phe-Trp-Thr-Ser-Ile-Asp-Val-Leu) and 2) to determine the effects of this antibody on the $\beta$-adrenergic receptor ligand interaction. The peptide sequence contains an amino acid residue such as Asp-113 which was identified as one of important component for receptor-ligand interaction in site-directed mutagenesis studies. Production of antibody was performed by immunization of rabbits through popliteal lymph node with the peptide coupled with Keyhole Limpet Hemocyanin (KLH). The titer of antibody against this peptide was 1 : 1000. The anti-peptide antibody was able to detect a 67 kDa protein band in western blot corresponding to the molecular weight of the $\beta$-adrenergic receptor in partially purified receptor fraction derived from guinea pig lung. The antisera inhibited the specific binding of [$^3$H]dihydroalprenolol to $\beta$-adrenergic receptor in a concentration-dependent manner. The results from this study suggest that the peptide sequence selected in the present study is important for the receptor ligand interaction.