The primary structure of initiation factor IF3 from Bacillus stearothermophilus

Makoto Kimura; Helmut Ernst; Krzysztof Appelt

doi:10.1016/0014-5793(83)80940-5

The primary structure of initiation factor IF3 from Bacillus stearothermophilus

Makoto Kimura, Helmut Ernst, Krzysztof Appelt

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

The complete amino acid sequence of the initiation factor IF3 from Bacillus stearothermophilus has been elucidated. This was achieved by splitting the protein with trypsin, Staphylococcus protease or cyanogen bromide. The amino acid sequence was determined by manual Edman degradation, using the DABITC/PITC double-coupling method. The IF3 molecule contains 171 amino acids and has an M_r of 19 677. The sequence was compared to the homologous molecule from Escherichia coli; about 50% of the amino acid residues were found to be identical.

Original language	English
Pages (from-to)	78-81
Number of pages	4
Journal	FEBS Letters
Volume	160
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(83)80940-5
Publication status	Published - Aug 22 1983
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(83)80940-5

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abstract = "The complete amino acid sequence of the initiation factor IF3 from Bacillus stearothermophilus has been elucidated. This was achieved by splitting the protein with trypsin, Staphylococcus protease or cyanogen bromide. The amino acid sequence was determined by manual Edman degradation, using the DABITC/PITC double-coupling method. The IF3 molecule contains 171 amino acids and has an Mr of 19 677. The sequence was compared to the homologous molecule from Escherichia coli; about 50% of the amino acid residues were found to be identical.",

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AU - Ernst, Helmut

AU - Appelt, Krzysztof

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AB - The complete amino acid sequence of the initiation factor IF3 from Bacillus stearothermophilus has been elucidated. This was achieved by splitting the protein with trypsin, Staphylococcus protease or cyanogen bromide. The amino acid sequence was determined by manual Edman degradation, using the DABITC/PITC double-coupling method. The IF3 molecule contains 171 amino acids and has an Mr of 19 677. The sequence was compared to the homologous molecule from Escherichia coli; about 50% of the amino acid residues were found to be identical.

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The primary structure of initiation factor IF3 from Bacillus stearothermophilus

Abstract

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