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Titolo:
PHOSPHORYLATION STATES OF ACTIN FILAMENT ADENINE-NUCLEOTIDES IN DETERGENT-EXTRACTED NEURONAL CYTOSKELETAL FRACTIONS
Autore:
ANGELASTRO JM; PURICH DL;
Indirizzi:
UNIV FLORIDA,HLTH SCI CTR,COLL MED,DEPT BIOCHEM & MOLEC BIOL GAINESVILLE FL 32610 UNIV FLORIDA,HLTH SCI CTR,COLL MED,DEPT BIOCHEM & MOLEC BIOL GAINESVILLE FL 32610
Titolo Testata:
Biochemical and biophysical research communications
fascicolo: 3, volume: 201, anno: 1994,
pagine: 1490 - 1494
SICI:
0006-291X(1994)201:3<1490:PSOAFA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
9
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Angelastro e D.L. Purich, "PHOSPHORYLATION STATES OF ACTIN FILAMENT ADENINE-NUCLEOTIDES IN DETERGENT-EXTRACTED NEURONAL CYTOSKELETAL FRACTIONS", Biochemical and biophysical research communications, 201(3), 1994, pp. 1490-1494

Abstract

High performance liquid chromatography of nucleotides from Triton X-100 cytoskeletal extracts has permitted analysis of the ATP and ADP content of actin filaments isolated intact from PC12 pheochromocytoma cells. We observed that the adenine nucleotide content matched the actin content of these cytoskeletal extracts, a finding consistent with the unit stoichiometry of nucleotide binding. Efficient assembly-linked ATP hydrolysis occurs in vivo, and based on a boundary hydrolysis model for nucleotide-promoted assembly, the observed ADP/ATP ratio indicatesthat the average microfilament in nonmuscle cells has 24 ATP-actin molecules at its growing end. Studies with NB41A3 neuroblastoma cells indicate that the ATP content of assembled actin filaments is about 3-4 times lower. (C) 1994 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 06:33:39