Biochemical and mass spectrometric characterization of soluble ecto-5'-nucleotidase from bull seminal plasma

Autor: Lino Ferrara, Fabio Talamo, Carlo Fini, Andrea Scaloni, Marcello Coli, Silvia Cherri, Ardesio Floridi

Publikováno v: Biochemical Journal. 372:443-451

Ecto-5′-nucleotidase (ecto-5′-NT) is a glycosylphosphatidylinositol-anchored membrane-bound protein that is ubiquitous in mammalian tissues. It is a target for a number of therapeutic drugs since increased levels of the enzyme correlate with vari

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ea27b2270079b971ceef3e157edbc00
https://doi.org/10.1042/bj20021687

The ecto-5′-nucleotidase subunits in dimers are not linked by disulfide bridges but by non-covalent bonds

Autor: José Neptuno Rodríguez-López, Encarnación Muñoz-Delgado, Francisco J. Campoy, Carlo Fini, Cecilio J. Vidal, César Flores-Flores, Alejandro Martínez-Martínez

Publikováno v: Europe PubMed Central

It has long been considered that ecto-5′-nucleotidase (eNT) dimers consist of subunits linked by disulfide bonds. Hydrophilic (6.7S) and amphiphilic (4.0S) dimers were separated by sedimentation analysis of eNT purified from bull seminal plasma. Hy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed45ba3546f7d23aa5e38f2a74950729
https://doi.org/10.1016/s0167-4838(00)00035-2

Expression and Enzymic Activity of Ecto 5′-Nucleotidase in the Human Male Genital Tract1

Autor: Gunther Wennemuth, Lutz Konrad, Gerhard Aumüller, Peter Schiemann, Carlo Fini, Heiner Renneberg

Publikováno v: Biology of Reproduction. 59:190-196

Human 5'-nucleotidase (5'-NT, EC 3.1.3.5) is an enzyme that hydrolyzes nucleotides such as AMP or IMP (inosine 5'-monophosphate) into inorganic phosphate and the respective nucleoside. It has been suggested that the enzyme acts as a scavenger of inju

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cab8945d0ff0efc00076027a15bc6079
https://doi.org/10.1095/biolreprod59.1.190

Structural and functional relationships in 5′-nucleotidase from bull seminal plasma. A Fourier transform infrared study

Autor: Fabio Tanfani, Ardesio Floridi, Enrico Bertoli, Carlo Fini, Gianni Albertini

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1118:187-193

Fourier transform infrared spectroscopy (FTIR) was used to investigate the secondary structure of 5'-nucleotidase from bull seminal plasma (BSP). Spectra of protein in both D2O and H2O were analyzed by deconvolution and second derivative methods in o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42b23013c289f47a7ba3d71cfd979e8a
https://doi.org/10.1016/0167-4838(92)90149-8

Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein

Autor: Mosè Rossi, Carlo Fini, Maria Staiano, Anna Marabotti, Sabato D'Auria, Konstantin K. Turoverov, Irina M. Kuznetsova, Olesya V. Stepanenko, Antonio Varriale

Publikováno v: Proteins (Online) 71 (2008): 35–44. doi:10.1002/prot.21658
info:cnr-pdr/source/autori:Stepanenko OV, Marabotti A, Kuznetsova IM, Turoverov KK, Fini C, Varriale A, Staiano M, Rossi M, D'Auria S./titolo:Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein./doi:10.1002%2Fprot.21658/rivista:Proteins (Online)/anno:2008/pagina_da:35/pagina_a:44/intervallo_pagine:35–44/volume:71

Despite the fact that the porcine odorant-binding protein (pOBP) possesses a single tryptophan residue (Trp 16) that is characterized by a high density microenvironment (80 atoms in a sphere with radius 7 A) with only one polar group (Lys 120) and th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f63435d224acbdd4594cb0219a72dfc
http://hdl.handle.net/11588/328926