G
Giampaolo Manao
Researcher at University of Florence
Publications - 73
Citations - 2747
Giampaolo Manao is an academic researcher from University of Florence. The author has contributed to research in topics: Acylphosphatase & Protein tyrosine phosphatase. The author has an hindex of 30, co-authored 73 publications receiving 2637 citations.
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Journal ArticleDOI
The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli.
TL;DR: Site directed mutagenesis suggests that, together with other structural features, the intrachain S–S bridge in EcoAcP is involved in a remarkable thermal and chemical stabilization of the protein without affecting its catalytic activity.
Journal Article
Turkey muscle acylphosphatase: purification and comparative studies.
Guido Camici,Giampaolo Manao,Massimo Stefani,Andrea Berti,Gianni Cappugi,Gianfranco Liguri,Giampietro Ramponi +6 more
TL;DR: Turkey muscle acylphosphatase is strongly bound to anti-horse muscle antibodies covalently linked to an agarose resin, which permits use of an affinity chromatography step in the purification, which increased the final yield and allowed us to isolate three different molecular forms of the enzyme.
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Heparin binding peptides co-purify with glycosaminoglycans from human plasma.
TL;DR: Progressive dilution of the sample allowed passage of peptides appearing as high molecular weight bands in the diffusate, interpreting this phenomenon as the presence of low molecular weight peptides that aggregate when concentrated.
Journal ArticleDOI
Rat muscle acylphosphatase: purification, amino sequence, and immunological characterization.
Andrea Berti,Elda Tremori,Luigia Pazzagli,Donatella Degl'Innocenti,Guido Camici,Gianni Cappugi,Giampaolo Manao,Giampietro Ramponi +7 more
TL;DR: Acylphosphatase was purified from rat skeletal muscle essentially by gel filtration and high-performance ion-exchange chromatography and revealed the presence of at least five antigenic sites on rat enzyme, two of which are common to horse muscle enzyme.
Journal ArticleDOI
The role of His66 and His72 in the reaction mechanism of bovine liver low-M(r) phosphotyrosine protein phosphatase.
Paola Chiarugi,Paolo Cirri,Guido Camici,Giampaolo Manao,Tania Fiaschi,Giovanni Raugei,Gianni Cappugi,Giampietro Ramponi +7 more
TL;DR: Site-directed mutagenesis of a synthetic gene coding for low-M(r) phosphotyrosine protein phosphatase from bovine liver has been carried out, with results strongly suggested by the results of diethyl pyrocarbonate inactivation of both single mutants.