• 제목/요약/키워드: L-serine

검색결과 259건 처리시간 0.051초

Effect of Low Molecular Weight Silk Fibroin on the Inhibition of Tyrosinase Activity

  • Kang, Gyung Don;Lee, Ki Hoon;Shin, Bong Seob;Nahm, Joong Hee;Park, Young Hwan
    • International Journal of Industrial Entomology and Biomaterials
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    • 제9권1호
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    • pp.29-33
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    • 2004
  • Low molecular weight silk fibroin (LMSF), which was prepared by hydrolysis of silk fibroin using high-temperature and high-pressure method, was found to inhibit the oxidation of L-3,4,-dihydroxyphenylalanine (L-DOPA) catalyzed by mushroom tyrosinase (EC 1.14.18.1). LMSF contained mostly free amino acids such as L-glycine, L-alanine, and L-serine and oligopeptides, mainly glycine-alanine dimer. As a result of analyzing the inhibition kinetics from Lineweaver-Burk plots, L-glycine and glycine-alanine dimer showed noncompetitive behavior while uncompetitive behavior was observed in L-alanine, and L-serine. When weight percent concentration of ${ID_50}$ was compared, L-glycine was most effective on the inhibition and LMSF was also good enough for the inhibition effect of tyrosinase activity. LMSF showed a mixed-type inhibition and the inhibitory mechanism of LMSF might be caused by free amino acids and oligopeptides. As a result of spectroscopic observation with time, initial rate of increase of DOPAchrome decreased remarkably and the time to reach maximum absorbance increased as an increase of the concentration of L-glycine, meaning that L-glycine made itself mainly responsible for the formation of chelate with ${Cu^2+}$ in tyrosinase. However, in case of L-alanine, L-serine, and especially glycine-alanine dimmer, the production of DOPAchrome after an arrival at maximum absorbance decreased, indicating the production of adducts through the reaction with DOPAquinone.

Streptomyces sp. YS-943균주가 생산하는 아미노산 대사길항물질의 정제와 성상 (Isolation and Properties of Amino Acid Antimetabolite from Streptomyces sp. YS-943)

  • 유성재;박부길
    • 한국미생물·생명공학회지
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    • 제23권1호
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    • pp.81-86
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    • 1995
  • A Streptomyces strain YS-943, which produced amino acid antimetabolite, was isolated from soil. During the course of screening for new amino acid antimetabolites from the culture broth of Actinomycetes, we found that the strain produced a substance active against Gram-positive bacteria and its activity was reversed by L-methionine and L-histidine on the synthetic minimal agar medium in the culture broth.The morphological and cultural characteristics serve to identify the producing organism strain YS-943 as the genus Streptomyces. Fermentation was carried out in the synthetic medium at 28$\CIRC$C for 48 hours. The fermentation yield reached about 12 mg per liter of the broth. The YS-943 substance was obtained as white powder, mp 194$\CIRC$C and has the molecular formular of C$_{4}$H$_{8}$N$_{2}$O$_{4}$. Its structure was determined to be o-carbamyl-D-serine by spectroscopic data. It is active against some Gram-positive bacteria and reversed by L-methionine and L-histidine.

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백서에서 Serine Protease 억제제가 난포성숙에 미치는 영향에 대한 연구 (Effect of Serine Protease Inhibitor on Follicular Development in the Rat Ovary)

  • 윤병구;이진용
    • Clinical and Experimental Reproductive Medicine
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    • 제20권1호
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    • pp.19-29
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    • 1993
  • Plasminogen activator (PA)-plasmin system in follicular fluid is involved in the process leading to follicular rupture at ovulation. It is well known that PA is closely associated with cellular differentiation and tissue remodeling on evidences from the study of normal and malignant tissues. This study was designed to ascertain a potential role of PA in the ovarian folliculogenesis. Immature Sprague-Dawley rats were injected with pregnant mare serum gonadotropin, followed by injection of serine protease inhibitor (SPI; mixture of 1 mol/L benzamidine and 1 mol/L amino-caproic acid) into the unilateral ovarian bursa. In the control study, mechanical effect of bursal injection and contralateral ovarian effect SPI were ruled out. Total antral follicular areas relative to total ovarian cross-sectional areas was siginificantly lower in SPI-injected ovary than in saline-injected ovary. SPI injection decreased the relative antral follicular area by 33 % respectively. Electron microscopic finding of granulosa cell in the atretic follicle showed the presence of pyknotic nucleus, blurring of neucleolemma, degeneration of mitochondria and dilation of endoplasmic reticulum. After induction of ovulation with hCG, the number of oocytes released was significantly decreased in SPI-injected oviduct than in saline-injected oviduct. From above results, author discussed that PA may play a role not only in ovulation but also in some processes of folliculogenesis.

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Stereoselective Synthesis of L-Deoxyaltronojirimycin from L-Serine

  • Rengasamy, Rajesh;Curtis-Long, Marcus J.;Ryu, Hyung-Won;Oh, Kyeong-Yeol;Park, Ki-Hun
    • Bulletin of the Korean Chemical Society
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    • 제30권7호
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    • pp.1531-1534
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    • 2009
  • (2S,3R)-3-Hydroxy-2-(hydroxymethyl)-3,6-dihydro-2H-pyridine 8, an important precursor for the synthesis of polyhydroxylated piperidine azasugars, has been prepared from L-serine. Highly stereoselective nucleophilic addition to amino aldehyde 5 gave the corresponding allylic alcohol 6 which proceeded to give dihydro-2H-piridine 7a via a Grubbs II catalyzed RCM. Stereoselective H-bond directed epoxidation of allylic alcohol led to the oxiranyl alcohol 9 which was easily converted to L-deoxyaltronojirimycin by regioselective ring opening.

Exoproduction and Biochemical Characterization of a Novel Serine Protease from Ornithinibacillus caprae L9T with Hide-Dehairing Activity

  • Li, Xiaoguang;Zhang, Qian;Gan, Longzhan;Jiang, Guangyang;Tian, Yongqiang;Shi, Bi
    • Journal of Microbiology and Biotechnology
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    • 제32권1호
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    • pp.99-109
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    • 2022
  • This study is the first report on production and characterization of the enzyme from an Ornithinibacillus species. A 4.2-fold increase in the extracellular protease (called L9T) production from Ornithinibacillus caprae L9T was achieved through the one-factor-at-a-time approach and response surface methodological optimization. L9T protease exhibited a unique protein band with a mass of 25.9 kDa upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This novel protease was active over a range of pH (4-13), temperatures (30-80℃) and salt concentrations (0-220 g/l), with the maximal activity observed at pH 7, 70℃ and 20 g/l NaCl. Proteolytic activity was upgraded in the presence of Ag+, Ca2+ and Sr2+, but was totally suppressed by 5 mM phenylmethylsulfonyl fluoride, which suggests that this enzyme belongs to the serine protease family. L9T protease was resistant to certain common organic solvents and surfactants; particularly, 5 mM Tween 20 and Tween 80 improved the activity by 63 and 15%, respectively. More importantly, L9T protease was found to be effective in dehairing of goatskins, cowhides and rabbit-skins without damaging the collagen fibers. These properties confirm the feasibility of L9T protease in industrial applications, especially in leather processing.

율무, 홍화, 아욱종자의 혈전용해 효소활성 및 감마선 조사의 영향 (Fibrinolytic Activities and Effects of Gamma-Irradiated on Seeds from Coix lacryma-jobi L. Carthamus tinctorius L. and Malva verticillata L.)

  • 권수정;임채영;김재성;박민희;이숙영
    • KSBB Journal
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    • 제21권1호
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    • pp.20-27
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    • 2006
  • 미생물 및 동물에 비해 식물에서는 혈전용해효소에 대한 연구가 부족한 실정이며, 기존의 혈전용해효소가 가지는 혈전에 대한 비특이적, 부작용, 고가 등의 단점을 해결할 수 있는 새로운 혈전용해효소의 개발을 위하여 율무, 홍화, 아욱의 종자로부터 추출된 수용성 단백질의 혈전용해 활성을 조사하였다. 각각의 식물들로부터 추출된 조효소 용액은 기존 혈전 용해효소인 plasmin과 양성 대조군으로 하여 비교하여 fibrin 평판법으로 확인한 결과 피브린 응집을 효과적으로 분해하였다. 그 중 율무종자의 수용성 추출물의 혈전용해 활성은 양성 대조군인 plasmin과 비교하여 1.3배의 높은 활성을 나타내었다. 전체 수용성 단백질은 50-75% 에탄올을 이용하여 농축하였으며 율무의 혈전용해효소는 fibrin zymography를 수행하여 확인하고 직접 추출하였다. SDS-PAGE에 의하여 추출효소의 분자량을 측정한 결과 7.8 kDa으로 단일 polypeptide임을 확인하였으며, 효소 활성에 미치는 온도의 효과는 $50^{\circ}C$ 이상에서는 비교적 안정하였으나 더 낮은 온도에서는 급격히 효소활성이 감소하였다. 또한, 각종 단백질분해효소 저해제에 의한 영향을 조사한 결과 APMSF, PMSF, pepstatin A 그리고 TPCK에 강력하게 저해되는 것으로 보아 추출효소는 chymotrypsin과 유사한 serine protease의 하나로 생각되었다. 그러나 EGTA와 EDTA 처리에 의해서는 효소활성의 저해가 두드러지게 나타나지 않았다. 더욱이, 종자저장 중에 미생물에 의한 부패, 활력저하, 생리활성물질의 감소와 장기저장에 따른 에너지소비 증가 등이 문제가 되고 있어 저선량의 감마선 조사를 통해 율무, 홍화, 아욱의 종자로부터 혈전용해 효소활성에 미치는 효과 및 선량에 따른 차이를 조사하였는데 비조사 종자인 대조구와 비교하여 1 Gy, 4 Gy, 16 Gy, 32 Gy선량에서는 낮은 활성을 보였으면 반면에 8 Gy와 64 Gy의 선량에서는 더 높은 활성을 나타내었다. 이러한 결과는 Y선 조사가 종자의 혈전용해 활성을 향상시킬 가능성이 있을 것으로 생각된다. 이상의 모든 결과로 볼 때 율무의 추출 효소는 chymotrypsin-like serine protease에 속하는 혈전용해효소임을 확인할 수 있었다.

아미노산을 리간드로 갖는 금속착화합물의 합성 및 반응성에 관한 연구(I) (The Study of Synthesis and Reactivity of Metal Complexes With Amino Acidic Ligands(I))

  • 한재홍;정평진
    • 한국응용과학기술학회지
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    • 제11권2호
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    • pp.75-87
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    • 1994
  • The metal complexes containing amino acidic ligands were prepared by using 11 kinds of amino acids as ligands and Ni, Cu, Co, Zn, Fe as a central metal. The starting was continued for 4hrs at room temperature. But Bis(D,L-Serine)Ni (II), and (D,L-Serine)Co (II) were prepared by heating method($80^{\circ}C$). In order to investigated reaction activity of Bis(D,L-Aspartato) Metal(II), stirring time was varied and Bis(D,L-Tyrosine ) Metal(II) used different divalent metal salts. We anticipate getting a great value from these prepared complexes as a monomer and a catalyst of polymerization which has peculier characteristics.

황색과 자색 양파의 화학성분 (Chemical Components of Yellow and Red Onion)

  • 정창호;김진희;심기환
    • 한국식품영양과학회지
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    • 제35권6호
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    • pp.708-712
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    • 2006
  • 황색과 자색 양파를 기능성식품 재료로 이용하기 위한 기초자료를 제공하기 위하여 화학성분을 조사하였다. 황색과 자색 양파의 수분 및 가용성 무질소물의 함량은 각각 92.80%, 5.13%와 92.47%, 5.59%로 나타났으며, 황색양파와 자색양파에 많이 함유되어 있는 무기성분으로는 K(123.64, 114.41 mg%), Na(34.09, 33.57 mg%) 및 Ca(18.77, 27.59 mg%)이었다. 황색양파의 주요 유리당은 glucose(744.2 mg%)와 fructose(705.9 mg%)였으며, 자색양파에서는 sucrose(692.8 mg%) 와 fructose(517.3 mg%)였다. 황색과 자색 양파의 총 아미노산 중 glutamic acid, phenylalanine 및 aspartic acid의 함량이 높았으며, 황색양파의 유리아미노산은 hydroxy-L-proline(27.34 mg%), L-serine(27.34 mg%) 및 L-arginine(26.25 mg%) 순이었고, 자색양파에서는 L-glutamic acid (16.35 mg%), ammonium chloride(15.22 mg%) 및 L-serine(10.93 mg%) 순이었다. 비타민 C 함량은 황색양파(19.20 mg%)보다 자색양파(28.34 mg%)가 높았으며, 황색과 자색양파의 quercetin 함량은 각각 15.24 mg%와 5.70 mg%였고, 총 폴리페놀 함량은 황색과 자색 양파에서 각각 0.319 mg/g 및 0.248 mg/g이었다.

Molecular Cloning, Gene Structure, Expression, and Enzyme Activity of a Serine Protease from Water Scorpion, Laccotrephes japonensis (Hemiptera: Nepidae)

  • Park, Kwan Ho;Choi, Young Cheol;Nam, Seong Hee;Hwang, Jae Sam;Nho, Si Kab
    • International Journal of Industrial Entomology and Biomaterials
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    • 제25권2호
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    • pp.187-193
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    • 2012
  • Serine proteases are major insect enzymes involved in the digestion of dietary proteins and in the process of blood meal digestion. In this study, cDNA was constructed using the whole body of Laccotrephes japonensis. The flanking sequences of the 5- and 3- end of this gene were characterized by RACE-PCR. Sequence analysis showed that this gene contained a 963-bp ORF encoding 320 amino acids. The deduced amino acid sequence showed 62% identity with the Creontiades dilutus serine protease, 58% with the Lygus lineolaris trypsin precursor, and 54% with the Triatoma infestans salivary trypsin. To assess the expression of the L. japonensis serine protease (JGsp), the JGsp gene was cloned into a baculovirus transfer vector, pBac-1, and expressed in Sf9 cells (Spodoptera frugiperda). SDS-PAGE and western blot analysis have shown that the JGsp recombinant protein was a monomer with a molecular weight of about 32 kDa. Recombinant JGsp has shown activity in the protease enzyme assay using gelatin as a substrate.

광학 활성 2-Amino-3-Phosphonopropionic Acid의 새로운 합성 방법과 그를 포함하는 펩티드의 합성 (Synthesis of Peptides Containing Optically Active 2-Amino-3-Phosphonopropionic Acid)

  • 김상범;조성기;한정식;김용준;홍석인
    • 대한화학회지
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    • 제38권7호
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    • pp.516-520
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    • 1994
  • L-serine으로부터 광학 활성을 가지는 2-amino-3-phosphonopropionic acid를 새로운 방법으로 합성하였으며 2-amino-3-(diethylphosphono)-propionic acid methyl ester를 아미노산과 축합시켜 광학 활성을 갖는 새로운 포스포노트리펩티드를 합성하였다.

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