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Titolo:
MAMMALIAN PHOSPHOLIPASE-D - ACTIVATION BY AMMONIUM-SULFATE AND NUCLEOTIDES
Autore:
NAKAMURA S; SHIMOOKU K; AKISUE T; JINNAI H; HITOMI T; KIYOHARA Y; OGINO C; YOSHIDA K; NISHIZUKA Y;
Indirizzi:
KOBE UNIV,SCH MED,DEPT BIOCHEM KOBE 650 JAPAN KOBE UNIV,BIOSIGNAL RES CTR KOBE HYOGO 650 JAPAN
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 26, volume: 92, anno: 1995,
pagine: 12319 - 12322
SICI:
0027-8424(1995)92:26<12319:MP-ABA>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
P(2Z) PURINERGIC RECEPTORS; PROTEIN-KINASE-C; BAC1.2F5 MACROPHAGES; PHOSPHATIDIC-ACID; NEUTROPHILS; HYDROLYSIS; MEMBRANE;
Keywords:
PHOSPHATIDYLCHOLINE; G PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
S. Nakamura et al., "MAMMALIAN PHOSPHOLIPASE-D - ACTIVATION BY AMMONIUM-SULFATE AND NUCLEOTIDES", Proceedings of the National Academy of Sciences of the United Statesof America, 92(26), 1995, pp. 12319-12322

Abstract

Phospholipase D (PLD) associated with the rat kidney membrane was activated by guanine 5'-[gamma-thio] triphosphate and a cytosol fraction that contained ADP-ribosylation factor, When assayed by measuring the phosphatidyl transfer reaction to ethanol with exogenously added radioactive phosphatidylcholine as substrate, the PLD required a high concentration (1.6 M) of ammonium sulfate to exhibit high enzymatic activity. Other salts examined were far less effective or practically inactive, and this dramatic action of ammonium sulfate is not simply due to such high ionic strength. Addition of ATP but not of nonhydrolyzable ATP analogue adenosine 5'-[beta,gamma-imido] diphosphate further enhanced the PLD activation approximate to 2- to 3-fold. This enhancement by ATP needed cytosol, implying a role of protein phosphorylation. A survey of PLD activity in rat tissues revealed that, unlike in previous observations reported thus far, PLD was most abundant in membrane fractions of kidney, spleen, and liver in this order, and the enzymatic activity in brain and lung was low.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 11:04:51