• 제목/요약/키워드: $Phospholipase\

검색결과 611건 처리시간 0.025초

Effect of Sodium deoxycholate and Sodium dodecy sulfate on Phospholipid Composition and Phospholiases of Rhizopus oryzae (Rhizopus oryzae의 인지질과 그 분해효소에 미치는 계면활성제의 영향)

  • 윤희주;조기승;최영길
    • Korean Journal of Microbiology
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    • 제24권1호
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    • pp.38-45
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    • 1986
  • Effect of sodium deoxycholate and sodium dodecyl sulfate on Rhizopus oryzae were investigated. Morphological change was obtained by supplement of these surfactants into culture media during the sumerged culture. In accordance with morphological changes, composition of phospholipid was changed. In case of surfactant-free culture, phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine were measured more than 95% of total phospholipid. But cardiolipin and phosphatidylinositol were conspicuously increased by treatment of both sufactants. Presence of phospolipase A, C, and D were detected from mycelium. Phospholipase A and D were activated by supplement of sodium deoxycholate and C was activated by sodium dodecyl sulfate. These results were interpreted in respect of polymorphism of phospholipid and membrane stability against solubilization effect of surfactants.

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Screening of the Extracts of Herbal Medicines which Stimulate the Hydrolysis of Phosphoinositides in Jurkat T-lymphocyte Cells (Jurkat T 면역세포에서 Phosphoinositides의 가수분해를 증가시키는 약용식물 추출물의 검색)

  • 민도식;이영한;백석환;서판길;류성호
    • Biomolecules & Therapeutics
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    • 제4권2호
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    • pp.148-153
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    • 1996
  • Activation of the T lymphocytes results in a variety of early biochemical events ultimately leading to cell proliferation and lymphokine production. Stimulation of the signal transduction cascade in T cells through the T cell receptor coincides with activation of the phosphatidylinositol-phospholipase C (PI-PLC) pathway. Therefore, we have established a model system to screen immune-simulator that can increase the hydrolysis of phosphoinositides in human T cell leukemia Jurkat cells. As a result of screening from herbal medicine extract, 4 extracts (O1ibanum, Ephedrae Herba, Real Gar, Saussureae Radix) were found 14 increase the production of inositol phosphates. All the active fraction from the four kinds of extract were fluted in a different retention time on C-18 HPLC and these active fraction also showed difference in cell specificity. And all the active fractions increased DNA synthesis in T cell. Therefore, it is suggested that the active fraction among 4 extracts might contain a compound having different properties one another.

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IDENTIFICATION AND CHARACTERIZATION OF PHOSPHOLIPASE $A_2$ IN OAT CELLS

  • Min, Youn-Mi;Choi, Eui-Chang;Chae, Quae
    • Journal of Photoscience
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    • 제2권1호
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    • pp.1-5
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    • 1995
  • The activity of phospholipase A$_2$ (PLA$_2$) was identified and characterized from cytosolic and membrane fractions of oat cells, respectively. PLA$_2$ activity was determined fluorometrically in the presence of serum albumin using phospholipids labeled at sn-2-acyl position with 10-pyrenyldecanoic acid. When the cell-free extracts of oat tissues were fractionated by ultracentrifugation at 100,000 x g and the PLA$_2$ activity was assayed, we found that most of the PLA$_2$ activity was revealed from the cytoplasmic fraction rather than from the membrane fraction. The activity of cytosolic PLA$_2$ was dependent on Ca$^{2+}$ concentration and the optimum concentration of Ca$^{2+}$ was found to be 100 $\mu$M. It was also found that PLA$_2$ could be translocated toward the membrane site from the cytosol upon increasing Ca$^{2+}$ concentration. These results might suggest that an increased [Ca$^{2+}$]$_i$ by phytochrome action could promote the translocation of the cytosolic PLA$_2$ toward the membrane site.

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Substrate Specificity of Cabbage Phospholipase D with Phospholipids Having Different Head Groups

  • 이지은;최명언
    • Bulletin of the Korean Chemical Society
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    • 제17권10호
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    • pp.905-908
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    • 1996
  • A substrate specificity of cabbage phospholipase D (PLD) was studied using the synthetic phospholipids having different head groups. The phospholipids were synthesized from phosphatidylcholine and appropriate bases by transphosphatidylation of PLD. The bases used were ethanolamine, serine, ethanol and γ-hydroxybutyric acid. The phosphatidic acid, the product of PLD, was separated in TLC and measured densitometrically. The kinetic parameters were estimated for each substrate and the effects of pH, SDS, Ca2+ and other metal ions were examined. Vmax values found were 3.75, 2.36, 5.59, 1.63, 2.30 nmol/min/μg protein for phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylethanol, and phosphatidylburytic acid, respectively. These results indicate a broad specificity of cabbage PLD toward phospholipids with different head groups. Particularly phosphatidylserine was most easily hydrolyzed by PLD and its activity did not depend on Ca2+.

Enzymatic Hydrolysis of p-Nitrophenyl Phsphoryl Derivatives by Phospholipase D

  • Cha, Joo-Yeun;Lee, Ji-Eun;Koh, Eun-Hie;Choi, Myung-Un
    • Bulletin of the Korean Chemical Society
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    • 제15권11호
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    • pp.1001-1003
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    • 1994
  • A series of phosphodiesters of p-nitrophenyl phosphoryl derivatives were synthesized and used as a model substrate for phospholipase D (PLD). The phosphodiester substrates were synthesized from p-nitrophenyl phosphorodichloridate and corresponding alcohols with different chain lengths and polar groups. To measure the activity of PLD, either spectroscopic method for p-nitrophenol or pH-stat titration method was employed. For each substrate, effects of substrate concentration, pH, and $Ca^{2+}$ ion were examined. The kinetic parameters $V_{max}$ for the different substrates were varied depending on the chain lengths or charge of the alcohols. No calcium effect was observed in the hydrolysis of neutral and negatively charged alcohol derivatives, while positively charged choline derivative showed a strong $Ca^{2+}$ ion dependence.

Large Unilamellar Phospholipid Vesicles as a Model Substrate for Phospholipase D

  • Kim Chanwoo;Koh Eun-Hie;Choi Myung-Un
    • Bulletin of the Korean Chemical Society
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    • 제13권4호
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    • pp.381-384
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    • 1992
  • The hydrolytic susceptibility of large unilamellar vesicle (LUV) toward cabbage phospholipase D (PLD) was studied. The activity of PLD was determined by pH stat titration method. Using phosphatidylcholine LUV as substrate a pH optimum of 6.96 was observed. For maximal activity the optimal temperature of $31^{\circ}C$ and 10 mM of Ca2+ were required. The apparent Km value estimated was 2.5 mM. The hydrolytic activity of PLD toward PC LUV was somewhat high despite the absence of activator in assay system and this high susceptibility of PC LUV may be attributed to the structural properties of LUV. The effect of amphiphatic substances such as dicetyl phosphate and phosphatidic acid on the enzyme activity were also examined in mixed LUVs.

Catalytic Properties of Phospholipase D using Phosphatidic Acid as an Activator

  • Eun-hie Koh;Myung-Un Chol;Kwanyoung Jung
    • Bulletin of the Korean Chemical Society
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    • 제10권6호
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    • pp.595-599
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    • 1989
  • The effects of phosphatidic acid(PA) on the activity of phospholipase D were examined in detail. The enzyme activity was examined in the liposome system containing phosphatidylcholine and PA, which was suspended in a desired buffer solution by ultrasonication. The substrate of large unilamella vesicle (LUV) state by ultrasonication was more effective on the enzyme activity than that of multilamella vesicle(MLV) by water-bath type sonication. The most effective molar ratio of PC-PA liposome for enzyme activity was found to be 1:0.7. The other optimum conditions were found 5 mM $Ca^{2+}$ ion, pH 6.6, and incubation temperature of $27^{\circ}C. K_m \;and \;V_{max}$ values were estimated to be 1.43 mM and 0.8 $nmole/min/{\mu}g$ protein respectively. These properties in a PC-PA liposome system were compared with those in a PC-SDS mixed micelle system. The effects of other phospholipids and organic phosphates on the enzyme activity were also examined.

Panaxadiol and Panaxatriol from Panax ginseng C.A. Meyer Inhibit the Synthesis of Thromboxane $A_2$ in Adrenaline-Stimulated Human Platelet Aggregations (Panax ginseng C.A. Meyer의 PD와 PT는 아드레날린에 의해 유인된 사람 혈소판의 응집반응에서 Thromboxane $A_2$의 생성을 저해한다)

  • Park, Kyeong-Mee;Rhee, Man-Whee;Park, Hwa-Jin
    • Journal of Ginseng Research
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    • 제18권1호
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    • pp.44-48
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    • 1994
  • In adrenaline-stimulated human platelets, panaxadiol (PD) and panaxatriol (PT) from Panax ginseng C.A. Meyer did not inhibit the $Ca^{2+}$-innux, but inhibited the formation of thromboxane $A_2$ and the platelet aggregations. It seems that PD and PT block a pathyway interconvefing arachidonic acids (20:4) to thromboxane $A_2$ (TX $A_2$), because the amount of $Ca^{2+}$ which phospholipase C or phospholipase $A_2$ requires to liberate 20 : 4 from membrane phospholipids was increased by PD and PT. These results mean that PH and PT have an antiplatelet effect by Inhibiting the formation of TX $A_2$.

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Enzymatic degumming of edible fats and oils (효소를 이용한 식용유지의 탈검 공정)

  • Yoon, Suk Hoo
    • Food Science and Industry
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    • 제51권2호
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    • pp.100-113
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    • 2018
  • To obtain an edible grade oil from crude oil extracted from oil-bearing materials, it is generally necessary to carry out a refining process composed with degumming, deacidification, bleaching, and deodorization, to remove undesirable matters which affect the quality and shelf life of oils. The main purpose of degumming is to remove gum material mainly consisted with phospholipids. Phospholipases convert nonhydratable phospholipids into their hydratable forms which can be removed by centrifugation. In comparison with conventional water and acid degumming processes, enzymatic degumming can result the lower phosphatide content in oil than conventional processes. The enzymatic degumming can be conducted with the reduced amount of acid, and contributes to generate less amount of wastewater, decrease of operating cost, and increase oil recovery yield. The phospholipases used in enzymatic degumming process are phospholipase A1, A2, B, and C.

Identification of a novel $Ca^{2+}$-independent Phospholipase $A_2$ in Bovine Brain

  • Jeong, Eui-Man;Jun, Hyung-Jin;Kim, Ha-Dong;Lee, Ho-Sup;Min, Pil-Gi;Jo, Dong-Hwan;Jung, Sung-Yun;Kim, Dea-Kyong
    • Proceedings of the PSK Conference
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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    • pp.102.1-102.1
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    • 2003
  • Phospholipase A$_2$(PLA$_2$) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid(AA), a precursor of eicosanoids including prostaglandins(PGs) and leukotrienes (LTs). The same reaction also produces lyso-phospholipids. So far, at least 19 enzymes that possess PLA2 activity have been identified, consists of low-molecular-weight, Ca$\^$2+/-requiring, secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, host defense, and atherosclerosis. (omitted)

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