• Title/Summary/Keyword: C-peptide

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Production and Separation of Angiotension Converting Enzyme Inhibitor during Natto Fermentation (납두 발효과정 중 Angiotensin Converting Enzyme 저해물질의 생성 및 분리)

  • Cho, Young-Je;Cha, Woen-Suep;Bok, Su-Kyung;Kim, Myung-Uk;Chun, Sung-Sook;Choi, Ung-Kyu;Kim, Soon-Hee;Park, Kyung-Sook
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.29 no.4
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    • pp.737-742
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    • 2000
  • As functionality investigation of a soybean fermentation food, a angiotensin converting enzyme inhibitory peptide was separated during natto fermentation by Bacillus natto and inhibitory effect was investigated. After incubation at each 2$0^{\circ}C$, 3$0^{\circ}C$, 4$0^{\circ}C$, 5$0^{\circ}C$, 6$0^{\circ}C$ for the 0~72 hr, protein content, protease activity and angiotensin converting enzyme inhibition were determined. The protein content and protease activity were increased and reached maximum at 60 hr fermentation with 4$0^{\circ}C$ and decreased after the 60 hr fermentation during natto fermentation. The optimum condition for angiotensin converting enzyme inhibitors was appeared at fermentation for 60 hr at 4$0^{\circ}C$. Crude extract of natto was partially purified by Amicon membrane YM-3 and Sephadex G-10, G-25 gel filtration, stepwise. The inhibitory rate was increased in a concentration dependent manner, espcially the most potent activity about 74.74% at 1.0 mg peptide content. The most prominent amino acid of the peptide from natto was alanine, followed by phenylalnine, histidine.

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Complement C5a Receptor Signaling in Macrophages Enhances Trained Immunity Through mTOR Pathway Activation

  • Eun-Hyeon Shim;Sae-Hae Kim;Doo-Jin Kim;Yong-Suk Jang
    • IMMUNE NETWORK
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    • v.24 no.4
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    • pp.24.1-24.8
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    • 2024
  • Complement C5a receptor (C5aR) signaling in immune cells has various functions, inducing inflammatory or anti-inflammatory responses based on the type of ligand present. The Co1 peptide (SFHQLPARSRPLP) has been reported to activate C5aR signaling in dendritic cells. We investigated the effect of C5aR signaling via the Co1 peptide on macrophages. In peritoneal macrophages, the interaction between C5aR and the Co1 peptide activated the mTOR pathway, resulting in the production of pro-inflammatory cytokines. Considering the close associations of mTOR signaling with IL-6 and TNF-α in macrophage training, our findings indicate that the Co1 peptide amplifies β-glucan-induced trained immunity. Overall, this research highlights a previously underappreciated aspect of C5aR signaling in trained immunity, and posits that the Co1 peptide is a potentially effective immunomodulator for enhancing trained immunity.

Antimicrobial Activity of Gluten Hydrolysate with Asp. saitoi Protease (밀 단백 효소 가수분해물의 항균활성)

  • Lee, Sang-Duk;Joo, Jeong-Hyeon;Lee, Gyu-Hee;Lee, K.T.;Oh, Man-Jin
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.32 no.5
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    • pp.745-751
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    • 2003
  • This study was carried out to investigate whether peptide produced from wheat protein by enzyme hydrolysis can be used as a natural antimicrobial agent. Antimicrobial peptide was obtained from wheat protein hydrolyzed by 7 of pretense. The produced antimicrobial peptide was purified through ultrafiltration, membrane filtration and HPLC and molecular weight and amino acid sequence of the purified antimicrobial peptide were determined. Among hydrolysate produced from wheat protein by 7 of protease, antimicrobial activity was observed for the peptide obtained from Asp. saito protease. The Asp. saito protease did produce antimicrobial hydrolysate showing the highest antimicrobial activity at reaction condition of 37$^{\circ}C$ and pH 6.0, but not at reaction condition above 5$0^{\circ}C$. Wheat protein hydrolysate was fractionated by membrane filtration and showed antimicrobial activity between molecular weight 1,000~3,000. The antimicrobial activity fraction obtained by membrane filtration was separated through HPLC and showed antimicrobial activity in the peak of retention time 31.1~31.8 min. We could convince this hydrolysate as heat-stable peptide since antimicrobial activity was maintained after treated with heat for 15 min at 121$^{\circ}C$. Molecular weight of antimicrobial peptide identified by MALDI-mass was 1,633. Amino acid sequence of antimicrobial peptide was cysteine, glycine, prolin, prolin, prolin, valine, valine, alanine, alanine and arginine.

Structural and Thermodynamic Characteristics of cHLH Peptide and cHLH/HDM2 Complex

  • Im, Haeri;Cho, Sunhee;Ham, Sihyun
    • Proceeding of EDISON Challenge
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    • 2016.03a
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    • pp.62-66
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    • 2016
  • Tumor suppressor protein p53 loses its function upon binding with the HDM2 protein, and inhibiting the p53-HDM2 interaction is critical to suppress tumor cell growth. Recently, the cyclized helix-loop-helix peptide (cHLH) mimicking the ${\alpha}-helix$ part of the p53 protein has been designed and found to exhibit high binding affinity with HDM2. Here, we report the structural and thermodynamic characteristics of the bound complex of the cHLH peptide with the HDM2 protein. We performed molecular dynamics simulations to investigate the structural features of the cHLH peptide as well as its complex with the HDM2. The binding free energy calculation based on the integral equation theory was also executed to quantify the binding affinity for the cHLH/HDM2 complex and to understand the factors contributing to the binding affinity. We found a variety of factors for the helix stability of the cHLH peptide as well as in the complexation with the HDM2, which may provide an insight into the development of anti-cancer drug designs.

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Peptide Production from the Washing Liquid of the Fish Paste of Alaska pollak (Theragria chalcogramma) by Immobilized Enzyme (고정화 효소를 이용한 명태고기풀 수세액으로부터 Peptide 생산에 관한 연구)

  • SHIN Suk-U;SUETSUNA Kunio
    • 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.

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Identification and Characterization of a Novel Antioxidant Peptide from Bovine Skim Milk Fermented by Lactococcus lactis SL6

  • Kim, Sang Hoon;Lee, Ji Yoon;Balolong, Marilen P.;Kim, Jin-Eung;Paik, Hyun-Dong;Kang, Dae-Kyung
    • Food Science of Animal Resources
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    • v.37 no.3
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    • pp.402-409
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    • 2017
  • A novel peptide having free radical scavenging activity was separated, using an on-line high-performance liquid chromatography (HPLC) - ABTS screening method, from bovine skim milk fermented by Lactococcus lactis SL6 (KCTC 11865BP). It was further purified using reverse phase-HPLC (RP-HPLC) and sequenced by RP-HPLC-tandem mass spectrometry. The amino acid sequence of the identified peptide was determined to be Phe-Ser-Asp-Ile-Pro-Asn-Pro-Ile-Gly-Ser-Glu-Asn-Ser-Glu-Lys-Thr-Thr-Met-Pro-Leu-Trp (2,362 Da), which is corresponding to the C-terminal fragment of bovine ${\alpha}_{s1}$-casein (f179-199). The hydroxyl radicals scavenging activity ($IC_{50}$ $28.25{\pm}0.96{\mu}M$) of the peptide chemically synthesized based on the MS/MS data showed a slightly lower than that of the natural antioxidant Trolox ($IC_{50}$ $15.37{\pm}0.52{\mu}M$). Furthermore, derivatives of the antioxidant peptide were synthesized. The antioxidative activity of the derivatives whose all three proline residues replaced by alanine significantly decreased, whereas replacement of two proline residues in N-terminal region did not affect its antioxidative activity, indicating that $3^{rd}$ proline in C-terminal region is critical for the antioxidative activity of the peptide identified in this study. In addition, N-terminal region of the antioxidant peptide did not show its activity, whereas C-terminal region maintained antioxidative activity, suggesting that C-terminal region of the peptide is important for antioxidative activity.

A novel nicotinoyl peptide, nicotinoyl-LVH, for collagen synthesis enhancement in skin cells

  • Kim, Hyoung Shik;Ryu, Seung Hwan;Kim, Hye In;Cho, Seung Hee;Lee, Jeong Hun;Han, Byung Suk;Lee, Kyung Rok;Moh, Sang Hyun
    • Journal of Applied Biological Chemistry
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    • v.59 no.3
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    • pp.239-242
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    • 2016
  • A novel Nicotinoyl fused peptide, Nicotinoyl-LVH, was synthesized by solid phase peptide synthesis method, purified, and tested in cultured skin cells. Nicotinoyl-LVH enhanced the expression level of collagen mRNA and its fragments in fibroblasts. These data show that this novel Nicotinoyl peptide is a promising biomaterial in the anti-aging functional cosmetic market.

Effects of Shudihuang Water Extracts on the cGMP Production and Receptors for Atrial Natriuretic Peptide in the Kidney in Rats (숙지황 전탕액이 백서의 신장내 cGMP 생성과 ANP 수용체에 미치는 영향)

  • Lee Ho Sub;Yu Yun Cho
    • Journal of Physiology & Pathology in Korean Medicine
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    • v.16 no.3
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    • pp.490-494
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    • 2002
  • The purpose of this study is to investigate the effect of Shudihuang water extracts on the cGMP production of medulla and cortical membranes, receptors for atrial natriuretic peptide in the kidney by in vitro autoradiography in rats for 8, 16 weeks. The cGMP production of medullary and cortical membranes of the kidney decreased after the administration of Shudihuang water extracts. The density of receptors for atrial natriuretic peptide in the kidney decreased after the administration of Shudihuang water extracts only for 16 weeks. These results suggest that the long term administration of Shudihuang water extracts has decreased plasma renin activity and plasma levels of aldosterone modulated cGMP production of medullary and cortical membranes, density of receptors for atrial natriuretic peptide in the kidney.

Stability of Separated ACE Inhibitory Peptides under Condition of Various pH, Temperature, Gastric Digestion (In Vitro)

  • Jang, Ae-Ra;Lee, Moo-Ha
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • 2005.10a
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    • pp.329-333
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    • 2005
  • ACE inhibition activity of peptides was measured after 2 months of storage at $4^{\circ}C$ under condition of pH 6.0, 6.5, 7.0, 7.5, 8.0. and the ACE inhibitory activity were changed only slightly. After 2 months of chilled storage ($4^{\circ}C$), no dramatic change and significance was found. This indicates that acidic, neutral, weak alkali conditions did not affect ACE inhibitory activity of those peptides. Among peptide 1134, 1152, and 1155, peptides from thermolysin + protease A hydrolysates, inhibition activity of peptide 1134 and 1152 was decreased significantly at $60^{\circ}C$, however, they showed stable inhibition activity from $70^{\circ}C$ to $100^{\circ}C$ (P<0.001). Also, chromatogram of peptide 1134, 1152, and 1155 was shown that retention time of peptide of $60^{\circ}C$ was not correspond to the retention time of the rest of peptides. This indicated that temperature may change the inhibitory activity and profile of peptides.

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A Study of the Insulin and the C-Peptide Responses to Oral Glucose Load in Nondiabetic and Diabetic Subjects (정상인(正常人) 및 당뇨병환자(糖尿病患者)에서의 경구당부하시(經口糖負荷時) 혈중(血中) Insulin과 C-Peptide의 변동(變動))

  • Lee, Myung-Chul;Choi, Sung-Jae;Kim, Eung-Jin;Min, Hun-Ki;Koh, Chang-Soon
    • The Korean Journal of Nuclear Medicine
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    • v.11 no.1
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    • pp.17-32
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    • 1977
  • The present study was undertaken to evaluate the significance of the insulin and the C-peptide rseponse to oral glucose loads in normal and diabetic subjects and to establish the effects of the obesity. In this study, the authors have measured plasma insulin and C-peptide by means of radioimmunoassay in 10 nonobese normal, 5 obese normal, 13 nonobese moderate diabetic patients, 9 obese moderate diabetic patients and 9 severe diabetic patients. The results obtained were as follows; 1. In 10 nonobese normal subjects, the plasma insulin level at fasting state and at 30, 60, 90, and 120 min after oral glucose loads were $15.7{\pm}3.4,\;48.3{\pm}9.8,\;40.4{\pm}6.7,\;37.4{\pm}6.5\;and\;26.0{\pm}4.2uU/ml(Mean{\pm}S.E.)$ and C-peptide were $1.9{\pm}0.3,\;3.9{\pm}0.6,\;6.3{\pm}0.6,\;5.7{\pm}0.5\;and\;4.0{\pm}0.5ng/ml$. The change of C-peptide was found to go almost parallel with that of insulin and the insulin value reaches to the highest level at 30 min whereas C-peptide reaches to its peak at 60min. 2. The plasma insulin level in 5 obese normal subjects were $38.9{\pm}12.3,\;59.5{\pm}12.3,\;59.2{\pm}17.1,\;56.1{\pm}20.0\;and\;48.4{\pm}17.2uU/ml$ and the C-peptide were $5.5{\pm}0.4,\;6.8{\pm}0.5,\;7.9{\pm}0.8,\;7.9{\pm}0.8\;and\;7.8{\pm}2.0ng/ml$. The insulin response appeared to be greater than nonobese normal subjects. 3. In 13 nonobese moderate diabetic patients, the plasma insulin levels were $27.1{\pm}4.9,\;44.1{\pm}6.0,\;37.3{\pm}6.6,\;35.5{\pm}8.1\;and\;34.7{\pm}10.7uU/ml$ and the C-peptide levels were $2.7{\pm}0.4,\;4.9{\pm}0.7,\;6.5{\pm}0.5,\;7.0{\pm}0.3\;and\;6.7{\pm}1.0ng/ml$. There was little significance compared to nonobese normal groups but delayed pattern is noted. 4. In 9 obese moderated diabetic patients, the plasma insulin levels were $22.1{\pm}7.9,\;80.0{\pm}19.3,\;108.0{\pm}27.0,\;62.0{\pm}17.6\;and\;55.5{\pm}10.1uU/ml$ and the C-peptide levels were $5.2{\pm}0.4,\;8.0{\pm}1.0,\;10.4{\pm}1.6,\;10.4{\pm}1.7\;and\;10.1{\pm}1.0ng/ml$ and its response was also greater than that of nonobese moderate diabetic patients. 5. The plasma insulin concentrations in 9 severe diabetic subjects were $8.0{\pm}3.8,\;12.1{\pm}3.5,\;16.8{\pm}4.6,\;19.6{\pm}5.2\;and\;15.0{\pm}5.0uU/ml$ and the C-peptide levels were $1.6{\pm}0.3,\;2.4{\pm}0.4,\;4.1{\pm}0.6,\;4.0{\pm}0.8\;and\;4.5{\pm}0.7ng/ml$ and the insulin and C-peptide responses were markedly reduced in severe diabetic groups. 6. There were-significant differences between each groups of patients on the magnitude of total insulin or C-peptide areas, the insulinogenic index and the C-peptide index.

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