Paolo Arcari | Università degli Studi di Napoli "Federico II" (original) (raw)

Papers by Paolo Arcari

Research paper thumbnail of Le Reazioni chimiche I

Research paper thumbnail of Composti Inorganici e nomenclatura

Research paper thumbnail of Acidi e basi

Research paper thumbnail of Proprietà delle soluzioni

Research paper thumbnail of Acetohydroxy Acid Synthase lsoenzymes of Escherichia coli K-12: A trans-Acting Regulatory Locus for ilvHl Gene Expression

Research paper thumbnail of Isolation of the human glyceraldehyde-3-phosphate dehydrogenase gene by hybridization with synthetic oligonucleotides

The Italian journal of biochemistry

By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synth... more By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synthetic oligonucleotides homologous to the human GAPD cDNA 3'-non-coding region as probes, a unique lambda recombinant clone (EMBL-G5) was isolated at the Tm value. Preliminary restriction analysis and sequence data proved that this recombinant clone is the human structural gene for the glyceraldehyde- 3-phosphate dehydrogenase.

Research paper thumbnail of Cloning of several cDNA segments coding for human liver proteins

The EMBO journal, 1983

A human cDNA library was constructed using M13 derivative vectors. The simple and rapid procedure... more A human cDNA library was constructed using M13 derivative vectors. The simple and rapid procedures for sequencing single-stranded DNA by the dideoxy chain termination method allowed a screening of individual clones directly by DNA sequence analysis. Some of these clones were identified as coding for: serum albumin, alpha1-antitrypsin, retinol-binding protein, prothrombin, haptoglobin, and metallothionein. Furthermore, a clone coding for aldolase B was tentatively identified on the basis of high sequence homology with rabbit muscle aldolase.

Research paper thumbnail of Isolation of the human glyceraldehyde-3-phosphate dehydrogenase gene by hybridization with synthetic oligonucleotides

The Italian journal of biochemistry

By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synth... more By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synthetic oligonucleotides homologous to the human GAPD cDNA 3'-non-coding region as probes, a unique lambda recombinant clone (EMBL-G5) was isolated at the Tm value. Preliminary restriction analysis and sequence data proved that this recombinant clone is the human structural gene for the glyceraldehyde- 3-phosphate dehydrogenase.

Research paper thumbnail of Studies on Transfer-Rna Patterns in Normal and Rous-Sarcoma Virus-Transformed Chick-Embryo Fibroblasts

Research paper thumbnail of Complete Sequence of Full-Length Cdna Coding for GLYCERALDEHYDE-3-PHOSPHATE Dehydrogenase from Human-Liver

Research paper thumbnail of Abundance of Pseudogenes for the Human GLYCERALDEHYDE-3-PHOSPHATE Dehydrogenase

Research paper thumbnail of Chromosomal Mapping by Insitu Hybridization of a Family of Sequences Related to GLYCERALDEHYDE-3-PHOSPHATE Dehydrogenase

Research paper thumbnail of Formation of uric acid from adenosylhomocysteine in rat liver

International Journal of Biochemistry, 1974

1. The metabolism of adenosyl-l-homocysteine (Ado-Hcy) has been investigated in rat liver homogen... more 1. The metabolism of adenosyl-l-homocysteine (Ado-Hcy) has been investigated in rat liver homogenate with the thioether labelled in the adenosine moiety or in the -COOH group. ... 2. Most of the radioactivity from the degradation of the [S- 14 C] adenosylhomocysteine in rat liver homogenate supernatant (cytoplasmic fraction) after dialysis, was found to be associated with a compound, which was isolated and identified as uric acid. ... 3. The time course of Ado-Hcy degradation and uric acid formation followed precursorproduct kinetics. ... 4. Under the same conditions adenosine, ...

Research paper thumbnail of Acetohydroxy acid synthase isoenzymes of Escherichia coli K-12: A trans-acting regulatory locus for ilvHI gene expression

MGG Molecular & General Genetics, 1981

Research paper thumbnail of Isoenergetic hydride transfer. A reversible, phase transition mediated tRNA modification

Journal of the American Chemical Society, 1977

The sample was mounted in a kel-F holder which masked all but a single, edge-oriented surface. Vo... more The sample was mounted in a kel-F holder which masked all but a single, edge-oriented surface. Voltammetric measurements were made using the graphite as working electrode in a three-electrode cell filled with 0.1 M tetrabutylammonium perchlorate in acetonitrile. In conventional cyclic voltammetry the faradaic current was poorly resolved from the very large capacitive component. Consequently, first-harmonic ac voltammetry was employed'using phase-selective rectification of the faradaic current.

Research paper thumbnail of The Importance of Climate for Dengue/DHF in Indonesia

Research paper thumbnail of Human glyceraldehyde-3-phosphate dehydrogenase pseudogenes: Molecular evolution and a possible mechanism for amplification

Biochemical Genetics, 1989

Research paper thumbnail of Abstract| Keywords| Fulltext| Export| TOC| Share

Research paper thumbnail of Archaeal elongation factor 1? from Sulfolobus solfataricus interacts with the eubacterial antibiotic GE2270A

Extremophiles, 2004

ABSTRACT The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from ... more ABSTRACT The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from Escherichia coli (EcEF-Tu), was used to study the effects produced in the biochemical properties of the archaeal functional analogue elongation factor 1alpha from Sulfolobus solfataricus (SsEF-1alpha). GE2270A did not substantially affect the poly(U)-directed-polyPhe incorporation catalyzed by SsEF-1alpha and the formation of the ternary complex SsEF-1alpha.GTP.Phe-tRNAPhe. On the other hand, the antibiotic was able to increase the GDP/GTP exchange rate of SsEF-1alpha; nevertheless, this improvement was not associated with an increase in the catalytic activity of the enzyme. In fact, GE2270A inhibited both the intrinsic GTPase of SsEF-1alpha (GTPaseNa) and that stimulated by ribosomes. Interestingly, GTPaseNa of both intact and C-terminal-deleted SsEF-1alpha resulted in a greater sensitivity to the antibiotic with respect to SsEF-1alpha lacking both the M- and C-terminal domains. This result suggested that, similar to what is found for EcEF-Tu, the M domain of SsEF-1alpha is the region of the enzyme most responsible for the interaction with GE2270A. The different behavior observed in the inhibition of protein synthesis with respect to EcEF-Tu can be ascribed to the different adaptive structural changes that have occurred in SsEF-1alpha during evolution.

Research paper thumbnail of A 35 kDa NAD(P)H oxidase previously isolated from the archaeon is instead a thioredoxin reductase

Biochimie, 2004

A thioredoxin reductase (TrxR) has been identified in the hyperthermophilic archaeon Sulfolobus s... more A thioredoxin reductase (TrxR) has been identified in the hyperthermophilic archaeon Sulfolobus solfataricus (Ss). This enzyme is a homodimeric flavoprotein that was previously identified as NADH oxidase in the same micro-organism ('Biotechnol. Appl. Biochem. 23 (1996) 47'). The primary structure of SsTrxR is made of 323 amino acid residues and contains two putative betaalphabeta regions for the binding of FAD, and a NADP(H) binding consensus sequence in the proximity of a CXXC motif. These findings indicate that SsTrxR is structurally related to the class II of the pyridine nucleotide-disulphide oxidoreductases family. Moreover, the enzyme exhibits a NADP(H) dependent thioredoxin reductase activity requiring the presence of FAD. Surprisingly, the reductase activity of SsTrxR is reduced in the presence of a specific inhibitor of mammalian TrxR. This finding demonstrates that the archaeal enzyme, although structurally related to eubacterial TrxR, is functionally closer to eukaryal enzymes. Experimental evidences indicate that a disulphide bridge is required for the reductase but also for the NADH oxidase activity of the enzyme. These results are further supported by the significantly reduced activities exerted by the C147A mutant. The integrity of the CXXC motif is also involved in the stability of the enzyme.

Research paper thumbnail of Le Reazioni chimiche I

Research paper thumbnail of Composti Inorganici e nomenclatura

Research paper thumbnail of Acidi e basi

Research paper thumbnail of Proprietà delle soluzioni

Research paper thumbnail of Acetohydroxy Acid Synthase lsoenzymes of Escherichia coli K-12: A trans-Acting Regulatory Locus for ilvHl Gene Expression

Research paper thumbnail of Isolation of the human glyceraldehyde-3-phosphate dehydrogenase gene by hybridization with synthetic oligonucleotides

The Italian journal of biochemistry

By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synth... more By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synthetic oligonucleotides homologous to the human GAPD cDNA 3'-non-coding region as probes, a unique lambda recombinant clone (EMBL-G5) was isolated at the Tm value. Preliminary restriction analysis and sequence data proved that this recombinant clone is the human structural gene for the glyceraldehyde- 3-phosphate dehydrogenase.

Research paper thumbnail of Cloning of several cDNA segments coding for human liver proteins

The EMBO journal, 1983

A human cDNA library was constructed using M13 derivative vectors. The simple and rapid procedure... more A human cDNA library was constructed using M13 derivative vectors. The simple and rapid procedures for sequencing single-stranded DNA by the dideoxy chain termination method allowed a screening of individual clones directly by DNA sequence analysis. Some of these clones were identified as coding for: serum albumin, alpha1-antitrypsin, retinol-binding protein, prothrombin, haptoglobin, and metallothionein. Furthermore, a clone coding for aldolase B was tentatively identified on the basis of high sequence homology with rabbit muscle aldolase.

Research paper thumbnail of Isolation of the human glyceraldehyde-3-phosphate dehydrogenase gene by hybridization with synthetic oligonucleotides

The Italian journal of biochemistry

By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synth... more By screening a human genomic library from human lymphocyte DNA cloned in EMBL 3 vector with synthetic oligonucleotides homologous to the human GAPD cDNA 3'-non-coding region as probes, a unique lambda recombinant clone (EMBL-G5) was isolated at the Tm value. Preliminary restriction analysis and sequence data proved that this recombinant clone is the human structural gene for the glyceraldehyde- 3-phosphate dehydrogenase.

Research paper thumbnail of Studies on Transfer-Rna Patterns in Normal and Rous-Sarcoma Virus-Transformed Chick-Embryo Fibroblasts

Research paper thumbnail of Complete Sequence of Full-Length Cdna Coding for GLYCERALDEHYDE-3-PHOSPHATE Dehydrogenase from Human-Liver

Research paper thumbnail of Abundance of Pseudogenes for the Human GLYCERALDEHYDE-3-PHOSPHATE Dehydrogenase

Research paper thumbnail of Chromosomal Mapping by Insitu Hybridization of a Family of Sequences Related to GLYCERALDEHYDE-3-PHOSPHATE Dehydrogenase

Research paper thumbnail of Formation of uric acid from adenosylhomocysteine in rat liver

International Journal of Biochemistry, 1974

1. The metabolism of adenosyl-l-homocysteine (Ado-Hcy) has been investigated in rat liver homogen... more 1. The metabolism of adenosyl-l-homocysteine (Ado-Hcy) has been investigated in rat liver homogenate with the thioether labelled in the adenosine moiety or in the -COOH group. ... 2. Most of the radioactivity from the degradation of the [S- 14 C] adenosylhomocysteine in rat liver homogenate supernatant (cytoplasmic fraction) after dialysis, was found to be associated with a compound, which was isolated and identified as uric acid. ... 3. The time course of Ado-Hcy degradation and uric acid formation followed precursorproduct kinetics. ... 4. Under the same conditions adenosine, ...

Research paper thumbnail of Acetohydroxy acid synthase isoenzymes of Escherichia coli K-12: A trans-acting regulatory locus for ilvHI gene expression

MGG Molecular & General Genetics, 1981

Research paper thumbnail of Isoenergetic hydride transfer. A reversible, phase transition mediated tRNA modification

Journal of the American Chemical Society, 1977

The sample was mounted in a kel-F holder which masked all but a single, edge-oriented surface. Vo... more The sample was mounted in a kel-F holder which masked all but a single, edge-oriented surface. Voltammetric measurements were made using the graphite as working electrode in a three-electrode cell filled with 0.1 M tetrabutylammonium perchlorate in acetonitrile. In conventional cyclic voltammetry the faradaic current was poorly resolved from the very large capacitive component. Consequently, first-harmonic ac voltammetry was employed'using phase-selective rectification of the faradaic current.

Research paper thumbnail of The Importance of Climate for Dengue/DHF in Indonesia

Research paper thumbnail of Human glyceraldehyde-3-phosphate dehydrogenase pseudogenes: Molecular evolution and a possible mechanism for amplification

Biochemical Genetics, 1989

Research paper thumbnail of Abstract| Keywords| Fulltext| Export| TOC| Share

Research paper thumbnail of Archaeal elongation factor 1? from Sulfolobus solfataricus interacts with the eubacterial antibiotic GE2270A

Extremophiles, 2004

ABSTRACT The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from ... more ABSTRACT The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from Escherichia coli (EcEF-Tu), was used to study the effects produced in the biochemical properties of the archaeal functional analogue elongation factor 1alpha from Sulfolobus solfataricus (SsEF-1alpha). GE2270A did not substantially affect the poly(U)-directed-polyPhe incorporation catalyzed by SsEF-1alpha and the formation of the ternary complex SsEF-1alpha.GTP.Phe-tRNAPhe. On the other hand, the antibiotic was able to increase the GDP/GTP exchange rate of SsEF-1alpha; nevertheless, this improvement was not associated with an increase in the catalytic activity of the enzyme. In fact, GE2270A inhibited both the intrinsic GTPase of SsEF-1alpha (GTPaseNa) and that stimulated by ribosomes. Interestingly, GTPaseNa of both intact and C-terminal-deleted SsEF-1alpha resulted in a greater sensitivity to the antibiotic with respect to SsEF-1alpha lacking both the M- and C-terminal domains. This result suggested that, similar to what is found for EcEF-Tu, the M domain of SsEF-1alpha is the region of the enzyme most responsible for the interaction with GE2270A. The different behavior observed in the inhibition of protein synthesis with respect to EcEF-Tu can be ascribed to the different adaptive structural changes that have occurred in SsEF-1alpha during evolution.

Research paper thumbnail of A 35 kDa NAD(P)H oxidase previously isolated from the archaeon is instead a thioredoxin reductase

Biochimie, 2004

A thioredoxin reductase (TrxR) has been identified in the hyperthermophilic archaeon Sulfolobus s... more A thioredoxin reductase (TrxR) has been identified in the hyperthermophilic archaeon Sulfolobus solfataricus (Ss). This enzyme is a homodimeric flavoprotein that was previously identified as NADH oxidase in the same micro-organism ('Biotechnol. Appl. Biochem. 23 (1996) 47'). The primary structure of SsTrxR is made of 323 amino acid residues and contains two putative betaalphabeta regions for the binding of FAD, and a NADP(H) binding consensus sequence in the proximity of a CXXC motif. These findings indicate that SsTrxR is structurally related to the class II of the pyridine nucleotide-disulphide oxidoreductases family. Moreover, the enzyme exhibits a NADP(H) dependent thioredoxin reductase activity requiring the presence of FAD. Surprisingly, the reductase activity of SsTrxR is reduced in the presence of a specific inhibitor of mammalian TrxR. This finding demonstrates that the archaeal enzyme, although structurally related to eubacterial TrxR, is functionally closer to eukaryal enzymes. Experimental evidences indicate that a disulphide bridge is required for the reductase but also for the NADH oxidase activity of the enzyme. These results are further supported by the significantly reduced activities exerted by the C147A mutant. The integrity of the CXXC motif is also involved in the stability of the enzyme.