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Protein Synthesis Initiation Factors from ..

N2 - An eight step procedure was devised for the preparation of homogeneous rabbit reticulocyte IF M1. Mol wt determinations based on IF M1 activity (gel filtration and sucrose density gradient sedimentation) and based on IF M1 protein (low speed equilibrium sedimentation and sodium dodecyl sulfate gel electrophoresis) indicate that IF M1 is active as a single polypeptide chain of 65,000 mol wt. The amino acid composition of IF M1 was determined. There appear to be no unique features in the amino acid composition of IF M1, except perhaps an elevated proline content (6.9 mol %). The catalytic properties of purified IF M1 were similar to those previously reported from the authors' laboratory for crude preparations of IF M1. The sensitivity of IF M1 activity to N ethylmaleimide and heat (45°) inactivation was tested in two model reactions requiring minimal complementary factors: AUG directed fMet tRNA (f) binding to ribosomes; and poly(U) directed polyphenylalanine synthesis at 4 mM Mg2+ (IF M2A, IF M2B, EF 1, and EF 2 also required). IF M1 activity proved to be sensitive to both N ethylmaleimide and temperature (45°). In addition, a contaminant of partially purified IF M1 preparations was found which is capable of fMet tRNA(f) binding but is inactive in poly(U) directed polyphenylalanine synthesis at low Mg2+ concentration.

The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes.

An eight step procedure was devised for the preparation of homogeneous rabbit reticulocyte IF M1. Mol wt determinations based on IF M1 activity (gel filtration and sucrose density gradient sedimentation) and based on IF M1 protein (low speed equilibrium sedimentation and sodium dodecyl sulfate gel electrophoresis) indicate that IF M1 is active as a single polypeptide chain of 65,000 mol wt. The amino acid composition of IF M1 was determined. There appear to be no unique features in the amino acid composition of IF M1, except perhaps an elevated proline content (6.9 mol %). The catalytic properties of purified IF M1 were similar to those previously reported from the authors' laboratory for crude preparations of IF M1. The sensitivity of IF M1 activity to N ethylmaleimide and heat (45°) inactivation was tested in two model reactions requiring minimal complementary factors: AUG directed fMet tRNA (f) binding to ribosomes; and poly(U) directed polyphenylalanine synthesis at 4 mM Mg2+ (IF M2A, IF M2B, EF 1, and EF 2 also required). IF M1 activity proved to be sensitive to both N ethylmaleimide and temperature (45°). In addition, a contaminant of partially purified IF M1 preparations was found which is capable of fMet tRNA(f) binding but is inactive in poly(U) directed polyphenylalanine synthesis at low Mg2+ concentration.

Protein synthesis in rabbit reticulocytes

T1 - Purification and characterization of homogeneous protein synthesis initiation factor M1 from rabbit reticulocytes

de Haro, C., and S. Ochoa. “Mode of action of the hemin-controlled inhibitor of protein synthesis: studies with factors from rabbit reticulocytes.” Proceedings of the National Academy of Sciences of the United States of America. 75, no. 6 (1978): 2713-6.

Grosfeld, H., and S. Ochoa. “Purification and properties of the double-stranded RNA-activated eukaryotic initiation factor 3 kinase from rabbit reticulocytes.” Proceedings of the National Academy of Sciences of the United States of America. 77, no. 11 (1980): 6526-30.

Protein synthesis in rabbit reticulocytes ..

1978 x The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes

Mariano, T.M., J. Siekierka, and S. Ochoa. “Purification and properties of the guanine nucleotide exchange factor (GEF) from HeLa cells and its role in the initiation of protein synthesis.” Biochemical and biophysical research communications. 134, no. 3 (1986): 1160-6.

Regulation of protein synthesis in rabbit reticulocyte lysates by the heme-regulated protein kinase: inhibition of interaction of Met-tRNAfMet binding factor with another initiation factor in formation of Met-tRNAfMet.40S ribosomal subunit complexes.

Purification and characterization of initiation factor IF-E2 from rabbit reticulocytes
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28/06/2008 · Abstract

AB - An eight step procedure was devised for the preparation of homogeneous rabbit reticulocyte IF M1. Mol wt determinations based on IF M1 activity (gel filtration and sucrose density gradient sedimentation) and based on IF M1 protein (low speed equilibrium sedimentation and sodium dodecyl sulfate gel electrophoresis) indicate that IF M1 is active as a single polypeptide chain of 65,000 mol wt. The amino acid composition of IF M1 was determined. There appear to be no unique features in the amino acid composition of IF M1, except perhaps an elevated proline content (6.9 mol %). The catalytic properties of purified IF M1 were similar to those previously reported from the authors' laboratory for crude preparations of IF M1. The sensitivity of IF M1 activity to N ethylmaleimide and heat (45°) inactivation was tested in two model reactions requiring minimal complementary factors: AUG directed fMet tRNA (f) binding to ribosomes; and poly(U) directed polyphenylalanine synthesis at 4 mM Mg2+ (IF M2A, IF M2B, EF 1, and EF 2 also required). IF M1 activity proved to be sensitive to both N ethylmaleimide and temperature (45°). In addition, a contaminant of partially purified IF M1 preparations was found which is capable of fMet tRNA(f) binding but is inactive in poly(U) directed polyphenylalanine synthesis at low Mg2+ concentration.

The Next Generation of Cell-free Protein Synthesis | NEB

Regulation of protein synthesis in rabbit reticulocyte lysates: characteristics of inhibition of protein synthesis by a translational inhibitor from heme-deficient lysates and its relationship to the initiation factor which binds Met-tRNAf.

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