Abstract
Crude extracts from Artemia salina undeveloped embryos do not contain detectable elongation-factor-2 (EF2) kinase and endogenous ADP-ribosylating activities. Accordingly, EF2 purified from this source is an enzyme relatively free from phosphorylated and ADP-ribosylated forms. Endogenous ADP-ribosyltransferase activity appears only after purification of EF2. The affinities of EF2 and of ADP-ribosyl-EF2 for ribosomes from A. salina undeveloped embryos have been calculated by measuring the ability of the factors to inhibit the N-glycosidase activity of ricin on ribosomes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Diphosphate Ribose / metabolism
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Animals
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Artemia / enzymology
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Calcium-Calmodulin-Dependent Protein Kinases*
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Electrophoresis, Polyacrylamide Gel
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Elongation Factor 2 Kinase
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Gastrula / enzymology
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Isoelectric Point
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Peptide Elongation Factor 2
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Peptide Elongation Factors / isolation & purification
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Peptide Elongation Factors / metabolism*
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Phosphorylation
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Poly(ADP-ribose) Polymerases / metabolism
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Protein Kinases / metabolism
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Rats
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Ribosomes / metabolism*
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Sepharose / analogs & derivatives
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Sepharose / metabolism
Substances
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Peptide Elongation Factor 2
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Peptide Elongation Factors
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heparin-sepharose
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Adenosine Diphosphate Ribose
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Sepharose
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Poly(ADP-ribose) Polymerases
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Protein Kinases
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Eef2k protein, rat
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Calcium-Calmodulin-Dependent Protein Kinases
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Elongation Factor 2 Kinase