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645 results on '"QUAGLIARIELLO E"'

24. Rat liver mitochondria can synthesize nicotinamide adenine dinucleotide from nicotinamide mononucleotide and ATP via a putative matrix nicotinamide mononucleotide adenylyltransferase

Author

Maria Barile, Passarella, S., Danese, G., and Quagliariello, E.

Subjects
Male, Adenosine Diphosphate Ribose, Mitochondria, Liver, Hydrogen-Ion Concentration, NAD, Adenosine Monophosphate, Rats, Substrate Specificity, Diphosphates, Adenosine Triphosphate, Animals, Nicotinamide-Nucleotide Adenylyltransferase, NADP, Nicotinamide Mononucleotide
Abstract

In order to gain some insight into the mechanism by which nicotinamide nucleotides localize in mitochondria, NMN was added to rat liver mitochondria, with NAD synthesis tested both enzymatically and by means of HPLC. Evidence is given that the mitochondrial matrix contains a specific NMN adenylyltransferase (E.C. 2.7.7.1.), inhibited by PPi, AMP and ADP-ribose. Some features of this enzyme, including the substrate, pH and temperature dependence were also investigated.

Published
1996

25. A new detergent to purify CNS myelin basic protein isoforms in lipid-bound form

Author

Paolo Riccio, Bobba A, Quagliariello E, E. Romito, and Minetola M

Subjects
Gene isoform, Detergents, Biology, Myelin, Isomerism, Chaps, medicine, Animals, Phospholipids, Brain Chemistry, General Neuroscience, fungi, food and beverages, Cholic Acids, Myelin Basic Protein, Lipids, Myelin basic protein, Structure and function, medicine.anatomical_structure, Biochemistry, Solubilization, biology.protein, Neuroglia, Cattle, Spectrophotometry, Ultraviolet, Chromatography, Thin Layer, Hydroxyapatites
Abstract

We have previously shown that CNS myelin basic protein (MBP) can be purified in the lipid-bound, native-like form by using a procedure based on myelin solubilization with detergents at pH above 7, and on the filter-like use of hydroxyapatite to separate non-adsorbed MBP from other myelin proteins. Here, we report on the isolation of MBP in the zwitterionic detergent 3-((3-cholamidopropyl)dimethylammonio)-1-propane sulfonate (CHAPS), which does not interfere at 280 nm and can be removed by dialysis. This detergent appears to improve MBP purification and to be suitable for fluorescence and reconstitution studies that can be useful to understand both structure and function of MBP in its natural environment.

Published
1994

33. Estimation of protein secondary structure from circular dichroism spectra: a critical examination of the CONTIN program

Author

Bobba A, Cavatorta P, Attimonelli M, Riccio P, Masotti L, and Quagliariello E

Subjects
Protein Conformation, Circular Dichroism, Spectrum Analysis, Ribonuclease, Pancreatic, Software
Abstract

The computer program CONTIN uses the Provencher and Glöckner procedure to calculate protein secondary structure from circular dichroism spectra. We have tested this program with peptides and proteins in which unfolding was either induced by denaturing treatment or was already present. Results indicate that the program does not clearly discriminate between the ordered and the unordered states of a protein.

Published
1990

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