• Title/Summary/Keyword: divalent cation

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Effect of Cation and Ionic Strength on Dispersion and Coagulation of Hwangto and Clay Minerals (양이온의 종류와 농도에 따른 황토와 점토광물의 분산과 응집)

  • Park, Bo-Kyeong;Kim, Kyung-Min;Kim, Young-In;Yum, Seo-Yun;Lee, Jeong-Woo;Hyung, Seuug-Woo;Hwang, Jun-Ho;Kim, Yu-Mi;Kong, Mi-Hye;Kim, Cheong-Bin;Roh, Yul
    • Journal of the Mineralogical Society of Korea
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    • v.22 no.3
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    • pp.249-259
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    • 2009
  • The objective of this research was to find out the physical properties, such as dispersion and coagulation, of soil minerals depending on the types and concentrations of the cations in aqueous solution. Hwangto samples were obtained from 90 to 130 cm from surface at Jangdong-ri, Donggang-Myon, Naju, Chonnam Province. The clay fraction (< $2\;{\mu}m$) was separated by sedimentation method from the bulk soils. Both Hwangto and clay fractions, and the same samples after removal of amorphous and crystalline iron oxides were used in this experiment. The effect of 4 cations ($Na^+$, $K^+$, $Mg^{2+}$, $Ca^{2+}$) and their concentrations on settling speed and basal spacing of the minerals were observed to examine the physical properties of the soil and clay minerals. Hwangto mainly consisted of quartz, and the clay fractions consisted of kaolinite, illite, and vermiculite. The bulk soils contained 16.3 mg/kg of amorphous iron oxides and 436 mg/kg of crystalline iron oxides. Clay fractions were dispersed better than bulk soils due to their smaller particle size than that of the bulk samples in the aqueous solution. The bulk and clay samples were dispersed better when iron oxides were removed because of coating of minerals by the iron oxides. Clay minerals were settled faster as the charge and the concentration of cations added increased. The d-spacing of kaolinite and illite did not change when 4 types of cations were added. The d-spacing of vermiculite showed $14.04\;{\AA}$ when divalent cations were added while that of vermiculite showed $13.9\;{\AA}$ when monovalent cations were added. It may be attributed to the hydration radii of cations. This study indicated that both coating of iron oxides on minerals and types and concentrations of cations affect dispersion of minerals in solution and d-spacing of expanding clay minerals such as vermiculite.

Endogenous Phenoloxidase Purified from an Earthworm, Lumbricus rubellus (붉은 지렁이(Lumbricus rubellus) 체내로부터 정제한 Phenoloxidase)

  • 백승렬;조은정;유경희;김유삼;서정진;장정순
    • The Korean Journal of Zoology
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    • v.39 no.1
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    • pp.36-46
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    • 1996
  • An endogenous phenoloxidase (EPO) from earthworm, Lumbricus rubellus, has been purified and characterized. The purified EPO using ammonium sulfate fractionation, Blue-2, Phenyl-, and Q-sepharose chromatography steps was revealed in SDS-PAGE as a single protein banri with Mr. of 59 kl)a. A native strudure of the enzyme was examined with an in situ staining of a nondenatudng-PAGE using DL-dopa as a substrate. The result showed that a single band due to the EPO activity was located siighdy above a standard polypeptide with Mr. of 210 kl)a. These fads indicate that the EPO is an oligomeric enzyme. The presence of a monophenolase activity of the purified EPO, which hydroxylates tyrosine to dopa, was confirmed by observing dopachrome accumulation at 475 nm at PH 8.0 with a typical lag phase during 60 mm. of meausrement. A series of inhibition study has been performed for the enzyme with several divalent cation chelators such as phenyithiourea (Flu), 1, lO-phenanthroline, EDTA, and EGTA. Among them, only V'flj inhibited the enzyme with 1C0.5 of 65 MM, which indicated that copper was critical for the catalysis of EPO. The enzyme was maximally active at 35'C and pH 8.0 when L-dopa to dopachrome conversion was spectrophotometricaily monitored at 475 nm. The apparent Km values of P0 for L-opa were obtained as 1.86 mM and 13.8 mM at pH 6.5 and 8.0, respectively. The catalytic efficiencies at both pH were almost identical [(kat/Km)pH8.0/(kcat/Km)pH6.5 = O.92] while the Vmax at p11 8.0 was 6.6-fold higher than that at pH 6.5. This fact may indicate that pH affeds the catalysis at substrate and/or enzyme-substrate complex level rather than the enzyme itself. Taken together, the EPO was an oligomeric enzyme which did not require proteolysis for its activation. These results also indicated that the enzyme can exist, at least, in part as a latent form In vivo, which might be distinct from the prophenoloxidase activating system. Therefore, it is pertinent to consider that there must be certain regulatory molecules or phenomena in L. rubellus which make the 1,0 in a latent form in vivo before the foreign invasions.

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