Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
FREE ADP-RIBOSE IN HUMAN ERYTHROCYTES - PATHWAYS OF INTRAERYTHROCYTICCONVERSION AND NONENZYMATIC BINDING TO MEMBRANE-PROTEINS
Autore:
ZOCCHI E; GUIDA L; FRANCO L; SILVESTRO L; GUERRINI M; BENATTI U; DEFLORA A;
Indirizzi:
FREE UNIV BERLIN,SCH MED,INST BIOCHEM,VIALE BENEDETTO XV 1 W-1000 BERLIN 19 GERMANY FREE UNIV BERLIN,SCH MED,INST BIOCHEM,VIALE BENEDETTO XV 1 W-1000 BERLIN 19 GERMANY RESPHARMA PHARMACOL RES I-10125 TURIN ITALY SCI INST CHEM & BIOCHEM G RONZONI I-20133 MILAN ITALY
Titolo Testata:
Biochemical journal
, volume: 295, anno: 1993,
parte:, 1
pagine: 121 - 130
SICI:
0264-6021(1993)295:<121:FAIHE->2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; CYCLIC METABOLITE; RAT-LIVER; RIBOSYLATION; NAD+; MONO(ADP-RIBOSYLATION); GLYCOHYDROLASE; INVIVO; CELL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
E. Zocchi et al., "FREE ADP-RIBOSE IN HUMAN ERYTHROCYTES - PATHWAYS OF INTRAERYTHROCYTICCONVERSION AND NONENZYMATIC BINDING TO MEMBRANE-PROTEINS", Biochemical journal, 295, 1993, pp. 121-130

Abstract

We have previously identified free ADP-ribose (ADPR) as a normal metabolite in mature human erythrocytes. In this study the metabolic transformations of ADPR were investigated in both supernatants from erythrocyte lysates and intact erythrocytes, loaded with ADPR by means of a procedure involving hypotonic haemolysis and isotonic resealing. In both experimental systems, the main pathway was a dinucleotide pyrophosphatase-catalysed hydrolysis to yield AMP, which was readily converted into the adenylic and inosinic nucleotide pools. To a lesser extent, ADPR underwent conversion into a compound that was identified as ADP-ribulose (ADPRu), on the basis of m.s., n.m.r. spectroscopy and enzymic analysis. ADPRu was also susceptible to degradation by the dinucleotidepyrophosphatase, which was partially purified from erythrocyte lysates and characterized with respect to its substrate specificity. Isomerization of ADPR to ADPRu was markedly enhanced by ATP. Incubation of unsealed haemoglobin-free crythrocyte membranes with labelled ADPR did not cause any transformation of this nucleotide and resulted in its trichloroacetic acid- and formic acid-resistant binding to a number of membrane cytoskeletal proteins. These proteins include spectrin, glyceraldehyde 3-phosphate dehydrogenase (Ga3PDH), three proteins of molecular masses 98, 79 and 72 kDa, which apparently comigrate with bands 3, 4.1 and 4.2 respectively, and two additional proteins of molecular masses 58 and 41 kDa. Acid-resistant binding of ADPR, as well as of NAD+, to Ga3PDH was confirmed for the enzyme purified from human erythrocytes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 20:07:12