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PMID: 873902 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Characterization of reticulocyte release factor.

The Journal of biological chemistry ·Vol. 252 ·No. 13 ·1977-07-10 ·Pages 4514-20

Konecki DS, Aune KC, Tate W, Caskey CT

Abstract

The release factor (RF) of reticulocytes has been purified to greater than 75% homogeneity. The RF has a native molecular weight of 105,000 and subunit molecular weight of 56,500. The RF protein will bind to reticulocyte ribosomes in response to UAAA, UAGA, or UGAA and therefore participates in codon recognition. The fraction possess a ribosome-dependent GTPase activity. The RF is stimulated in its activity by a second protein fraction.

MeSH Terms

Animals Blood Protein Electrophoresis Blood Proteins/isolation & purification,metabolism Centrifugation, Density Gradient Chemical Phenomena Chemistry Chromatography, Gel Electrophoresis, Polyacrylamide Gel Guanosine Triphosphate/blood Hydrolysis In Vitro Techniques Molecular Weight Peptide Termination Factors/blood,isolation & purification Rabbits Reticulocytes/analysis,metabolism Ribosomes/metabolism

Chemicals

Blood Proteins Peptide Termination Factors Guanosine Triphosphate

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Konecki D S

Aune K C

Tate W

Caskey C T

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1977-07-10

Pages

4514-20

Language

English

Region

United States

NLM ID

2985121R

Subset

External Links

PubMed source View journal details

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