Purified eukaryotic initiation factor 2 from calf liver consists of two polypeptide chains of 48,000 and 38,000 daltons.

E. A. Stringer, A. Chaudhuri, U. Maitra

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Eukaryotic initiation factor 2 (eIF-2), which specifically binds Met-tRNAMetf and forms stable ternary complexes with GTP, has been purified from ribosomal salt wash proteins from calf liver. The purified factor exhibits only two polypeptide bands of Mr = 48,000 and 38,000 following electrophoresis in 15% polyacrylamide gels in the presence of sodium dodecyl sulfate. Densitometric tracings show the two polypeptides are present in a molar ratio of 1:1. This suggests a Mr = 86,000 for the native enzyme, a value which agrees with the apparent molecular weight determined by physical methods. Less pure preparations of eIF-2 show additional polypeptide bands, including 50,000- and 46,000-dalton bands, all of which can be removed by further purification without affecting the activity of eIF-2.

Original languageEnglish (US)
Pages (from-to)6845-6848
Number of pages4
JournalJournal of Biological Chemistry
Volume254
Issue number15
StatePublished - Aug 10 1979
Externally publishedYes

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Eukaryotic Initiation Factor-2
Liver
Peptides
Guanosine Triphosphate
Electrophoresis
Sodium Dodecyl Sulfate
Purification
Salts
Molecular Weight
Molecular weight
Enzymes
polypeptide 48
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purified eukaryotic initiation factor 2 from calf liver consists of two polypeptide chains of 48,000 and 38,000 daltons. / Stringer, E. A.; Chaudhuri, A.; Maitra, U.

In: Journal of Biological Chemistry, Vol. 254, No. 15, 10.08.1979, p. 6845-6848.

Research output: Contribution to journalArticle

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