Characterization of a Metal-Chelating Substance in Coffee

2005 ◽  
Vol 69 (1) ◽  
pp. 26-30 ◽  
Author(s):  
Makiko TAKENAKA ◽  
Naoko SATO ◽  
Hiromi ASAKAWA ◽  
Xu WEN ◽  
Masatsune MURATA ◽  
...  
Keyword(s):  
2009 ◽  
Vol 131 (4) ◽  
pp. 1436-1451 ◽  
Author(s):  
Cristina Rodríguez-Rodríguez ◽  
Natalia Sánchez de Groot ◽  
Albert Rimola ◽  
Ángel Álvarez-Larena ◽  
Vega Lloveras ◽  
...  

Modification of a membrane surface is critical to help further functional protein binding on the membrane. Mussel inspired modification and metal chelating agent grafting on the polyvinylidene fluoride (PVDF) is proposed to increase the hydrophilicity, stability, and functionality of the membrane. This study carried out a four steps modification including polymerization of dopamine, grafting with poly (ethyleneimine) (PEI) and metal chelating agent and finally metal (ZnO) coupling. Characterization of the modified membrane was carried out using contact angle observation, permeate flux analysis, FT-IR spectrum and FESEM analysis. The results show a successful PDA and PEI deposition on PVDF membrane with significant improvement of the membrane hydrophilicity and wettability. Permeate flux analysis showed blockage on membrane surface due to the successful coating. Absorption peak increased slightly showing the deposition of PDA/PEI. Successful Zn2+ ion coupling can be seen clearly from the FESEM analysis


Pteridines ◽  
1995 ◽  
Vol 6 (2) ◽  
pp. 58-62
Author(s):  
Young Shik Park ◽  
Nacksung Kim ◽  
Hajeong Kim ◽  
Dongkook Park ◽  
Jeongbin Yim

Summary 6-Pyruvoyl tetrahydropterin synthase is involved in the synthesis of pteridine eye pigments in Drosophila. The purple gene which was known to be one of the target loci of the suppressor mutation su(sj2 has been identified to encode the enzyme, and its cDNA has been cloned recently. The cDNA encoding the 19.3 kDa subunit of the 6-pyruvoyl tetrahydropterin synthase was expressed as fusion proteins in E. coli. The recombinant protein was shown to be active and purified from the E. coli crude extract by metal-chelation chromatography. The fused metal-chelating oilgopeptide was removed by thrombin for further characterization. Apparent Km for the substrate dihydroneopterin triphosphate was determined to be 590 IlM, which was slightly higher than the value of the native enzyme. The isoelectric point of 6.4 was also different from the known value of 4.3 determined by the native enzyme. Heat stability and the stimulatory effect of reducing agents were similar to the native enzyme. The modification of cysteine residues in the recombinant enzyme, one of which is known to be conserved in human and rat enzymes, by iodoacetamide inhibited its activity by up to 80%.


Author(s):  
Seiichi Homma ◽  
Yuki Nakamura ◽  
Tomiko Asakura ◽  
Nobuko Sekiguchi ◽  
Masatsune Murata

1980 ◽  
Vol 52 (6) ◽  
pp. 967-972 ◽  
Author(s):  
M. B. Colella ◽  
S. Siggia ◽  
R. M. Barnes

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