Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Franco Marmocchi"'
Publikováno v:
Electrochimica Acta. 50:2437-2443
Biological X-ray absorption spectroscopy (BioXAS) is able to describe the metal environment in a metalloprotein and is sensitive to metal oxidation state. Coupling of BioXAS and electrochemistry permits the characterization of different oxidation sta
Publikováno v:
Preparative Biochemistry and Biotechnology. 31:317-329
Bovine brain glyoxalase I was investigated in order to identify amino acid residues essential for its catalytic activity. This enzyme is a 44-kDa dimeric protein which exhibits a characteristic intrinsic fluorescence, with an emission peak centered a
Publikováno v:
Preparative Biochemistry and Biotechnology. 31:305-316
Glyoxalase I was purified to homogeneity from bovine brain using affinity chromatography on S-hexylglutathione-Sepharose 6B with a yield of 22%. The enzyme was a dimer (44,000 Daltons) composed of, apparently, identical subunits (22,000 Daltons), as
Autor:
Franco Marmocchi, G. Rotilio, Giorgio Pelosi, Martino Bolognesi, Mattia Falconi, Alessandro Coda, Giuseppina Gatti, K. Djinovic, L. Antolini, Alessandro Desideri
Publikováno v:
Journal of Molecular Biology. 225:791-809
The structure of Cu,Zn yeast superoxide dismutase has been determined to 2.5 A resolution. The enzyme crystallizes in the P21212 space group with two dimeric enzyme molecules per asymmetric unit. The structure has been solved by molecular replacement
Akademický článek
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Publikováno v:
Scopus-Elsevier
The ecto form of adenosine deaminase isolated from human placental membrane was tested towards its sensitivity against adenosine deaminase inhibitors, such as aza and deaza analogues of adenosine and erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA). Ki va
Autor:
Laura Cervoni, Franco Marmocchi, Anna Ferraro, Carlo Turano, Margherita Eufemi, Patrizia Ciavatta
Publikováno v:
FEBS letters. 417(2)
RNA polymerase II from wheat germ was analyzed for the presence of sugars. The two largest subunits and the 27 and 25 kDa subunits were found to be glycosylated by a variety of sugars. However, no N-acetylglucosamine was detected, which was found by
Publikováno v:
Scopus-Elsevier
Brain adenosine deaminase was investigated in order to identify amino acid residues essential for its catalytic activity. The pH dependence of log Vmax shows that the enzyme activity depends on two ionizing groups with pK values of 5.4, that must be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0605aa0179be3b0e4c3d1ba9187e9de7
http://hdl.handle.net/11581/113994
http://hdl.handle.net/11581/113994
Autor:
Alessandro Desideri, G. Aureli, A.M. Caccuri, Franco Marmocchi, A. Risitano, G. Venardi, Raffaele Petruzzelli
Glyoxalase I has been purified to homogeneity from Saccharomyces cerevisiae and tested with two different thiol reagents, i.e., 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and 1-chloro-2,4-dinitrobenzene (CDNB). DTNB reacts with four thiol groups per
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cea688be8d2c093d5734960397b69adf
http://hdl.handle.net/2108/68916
http://hdl.handle.net/2108/68916
Autor:
Edward P. Whitehead, Franco Marmocchi, F. Riva, Giulio Lupidi, G. Venardi, Gloria Cristalli, Mario Grifantini, Marco Falasca
Publikováno v:
Biochimica et biophysica acta. 1122(3)
Several adenosine analogs, such as coformycin, 2'-deoxycoformycin and erythro-9-(3-nonyl-p-aminobenzyl)adenine (EHNA), which are strong inhibitors of mammalian adenosine deaminase, are much weaker inhibitors of the Saccharomyces cerevisiae enzyme. Th