Preparation and Analysis of Basic Proteins

A peptidic effector from calf thymus causes a strong stabilization of DNA double-stranded molecule in vitro. The active factor was isolated from aqueous ultrafiltered thymus extracts and purified by means of chromatography on DEAE-cellulose and then on Dowex 50 WX2. The purified thymic factor was characterized as a peptide of low molecular weight (less than 5000). The biological activity of the thymic factor cannot be attributed to a histone fragment. Melting data of the control DNA and of the DNA-active factor complex in various conditions of ionic strength and dielectric constant of the solution medium are recorded.

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Stabilization of double-stranded DNA molecule by nonhistone peptidic effector from calf thymus

Gianfranceschi

Amici

Guglielmi

1976

Molecular Biology Reports

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Evidence for the presence in calf thymus of a peptidic factor controlling DNA transcription in vitro

Gianfranceschi

Amici

Guglielmi

1975

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein

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The composition of sea urchin sperm and embryo histones

Johnson

Wilhelm

Ward

et al. 1973

Biochimica et Biophysica Acta (BBA) - Protein Structure

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Preparation and Analysis of Basic Proteins

Cited by 10 publications

References 100 publications

Stabilization of double-stranded DNA molecule by nonhistone peptidic effector from calf thymus

Stabilization of double-stranded DNA molecule by nonhistone peptidic effector from calf thymus

Evidence for the presence in calf thymus of a peptidic factor controlling DNA transcription in vitro

The composition of sea urchin sperm and embryo histones

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