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Titolo:
A TYPE 2A PROTEIN PHOSPHATASE FROM CLAM SMOOTH-MUSCLE - USE OF 4-METHYLUMBELLIFERYL PHOSPHATE AS SUBSTRATE
Autore:
TSUCHIYA T; IKEDA N; OBARA K; HARTSHORNE DJ;
Indirizzi:
SOPHIA UNIV,FAC SCI & TECHNOL,DEPT CHEM,CHIYODA KU,7-1 KIOI CHO TOKYO102 JAPAN UNIV ARIZONA,MUSCLE BIOL GRP TUCSON AZ 85721
Titolo Testata:
Comparative biochemistry and physiology. B. Comparative biochemistry
fascicolo: 1, volume: 118, anno: 1997,
pagine: 17 - 21
SICI:
0305-0491(1997)118:1<17:AT2PPF>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
OKADAIC ACID; SERINE THREONINE; MICROCYSTIN-LR; CALYCULIN-A; INHIBITION; TAUTOMYCIN; CLASSIFICATION; POTENT; MYOSIN;
Keywords:
PROTEIN PHOSPHATASE TYPE 2A; MOLLUSCAN SMOOTH (CATCH) MUSCLE; 4-METHYLUMBELLIFERYL PHOSPHATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
T. Tsuchiya et al., "A TYPE 2A PROTEIN PHOSPHATASE FROM CLAM SMOOTH-MUSCLE - USE OF 4-METHYLUMBELLIFERYL PHOSPHATE AS SUBSTRATE", Comparative biochemistry and physiology. B. Comparative biochemistry, 118(1), 1997, pp. 17-21

Abstract

1) The major cytosolic protein phosphatase from clam (Meretrix lamarckii) smooth muscle was isolated by ion exchange and gel filtration chromatography 1) The isolation procedures were facilitated by use of thesensitive fluorescent substrate, 4-methylumbelliferyl phosphate. 3) The isolated phosphatase was a type 2A enzyme, as indicated by subunit composition and antigenic properties of the catalytic subunit. 4) In spite of some differences between the organic and protein substrates, 4-methylumbelliferyl phosphate offers an convenient alternative to the use of radioisotopes in phosphatase assays. (C) 1997 Elsevier Science Inc.

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Documento generato il 10/07/20 alle ore 03:10:26