Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins

P. Raychaudhuri, S. Ghosh, U. Maitra

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A potent guanosine diphosphatase activity that hydrolyzes GDP to 5'-GMP + P(i) has been isolated and purified from the salt wash proteins of calf liver microsomes. The purified enzyme, a monomeric protein of approximate M(r) 46,000, possesses nucleotide substrate specificity since, among the nucleoside diphosphates and triphosphates tested, only GDP and UDP are hydrolyzed by the enzyme. The relative affinity of the enzyme for GDP is, however, much higher than for UDP. The effect of the enzyme on the binary complex formed between eukaryotic initiation factor 2 (eIF-2) and GDP has also been investigated. The enzyme neither hydrolyzes GDP bound to eIF-2 nor catalyzes the exchange of eIF-2-bound GDP with GTP even in the presence of Met-tRNA(f). The enzyme, therefore, is presumably not involved in recycling of eIF-2 in eukaryotic polypeptide chain initiation reaction. The possible biological function of the enzyme in maintaining the cellular pool of GTP-GDP is discussed.

Original languageEnglish (US)
Pages (from-to)8306-8311
Number of pages6
JournalJournal of Biological Chemistry
Volume260
Issue number14
StatePublished - 1985

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Liver
Purification
Eukaryotic Initiation Factor-2
Salts
Enzymes
Proteins
Uridine Diphosphate
Guanosine Triphosphate
Guanosine Monophosphate
Diphosphates
Recycling
Liver Microsomes
Substrate Specificity
guanosine-diphosphatase
Nucleosides
Nucleotides
Peptides
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins. / Raychaudhuri, P.; Ghosh, S.; Maitra, U.

In: Journal of Biological Chemistry, Vol. 260, No. 14, 1985, p. 8306-8311.

Research output: Contribution to journalArticle

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N2 - A potent guanosine diphosphatase activity that hydrolyzes GDP to 5'-GMP + P(i) has been isolated and purified from the salt wash proteins of calf liver microsomes. The purified enzyme, a monomeric protein of approximate M(r) 46,000, possesses nucleotide substrate specificity since, among the nucleoside diphosphates and triphosphates tested, only GDP and UDP are hydrolyzed by the enzyme. The relative affinity of the enzyme for GDP is, however, much higher than for UDP. The effect of the enzyme on the binary complex formed between eukaryotic initiation factor 2 (eIF-2) and GDP has also been investigated. The enzyme neither hydrolyzes GDP bound to eIF-2 nor catalyzes the exchange of eIF-2-bound GDP with GTP even in the presence of Met-tRNA(f). The enzyme, therefore, is presumably not involved in recycling of eIF-2 in eukaryotic polypeptide chain initiation reaction. The possible biological function of the enzyme in maintaining the cellular pool of GTP-GDP is discussed.

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