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Journal ArticleDOI

Studies on acid hydrolases: IV. Isolation and characterization of spleen exonuclease

Alberto Bernardi, +1 more
- 26 Feb 1968 - 
- Vol. 155, Iss: 2, pp 360-370
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TLDR
Using acid deoxyribonuclease digest as the substrate, the pH optimum of the enzyme is close to 5.5 in succinate buffer, whereas a higher value is found in acetate buffer; pH-activity curves are barely affected by the presence of Mg2+.
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This article is published in Biochimica et Biophysica Acta.The article was published on 1968-02-26. It has received 81 citations till now. The article focuses on the topics: Phosphomonoesterase & Deoxyribonuclease.

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Mitochondrial DNA's from respiratory-sufficient and cytoplasmic respiratory-deficient mutant yeast.

TL;DR: The mitochondrial DNA's from two “grande” yeast strains and three cytoplasmic “petite” mutants were isolated by hydroxyapatite chromatography and investigated in their chemical and physical properties.
Journal ArticleDOI

Chromatography of polypeptides and proteins on hydroxyapatite columns: some new developments.

TL;DR: Findings of the present work very strongly support the idea that crystals have two different adsorption sites on their surface, to be identified with phosphate and calcium, and that these are responsible for the binding of basic and acidic side groups of proteins, respectively.
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Mechanism of DNA chain growth XVI. Analyses of RNA-linked DNA pieces in Escherichia coli with polynucleotide kinase.

TL;DR: In this paper, an improved method for the isolation of RNA-linked DNA pieces from Escherichia coli was developed, which strongly suggests that the short RNA segment is covalently linked to the 5′ end of DNA.
Journal ArticleDOI

Properties of Deoxyribonuclease III from Mammalian Tissues

TL;DR: A DNA exonuclease, DNase III, has been purified 680-fold from normal rabbit bone marrow and appears to be the predominant DNA ex onuclease in many different mammalian tissues.
References
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Journal ArticleDOI

The deoxyribonucleases of Escherichia coli. I. Purification and properties of a phosphodiesterase.

TL;DR: The purpose of this report is to describe in detail the purification and properties of this enzyme which will be referred to as the Escherichia coli phosphodiesterase, found to hydrolyze E. coli and calf thymus DNA’s to their constituent 5’-mononucleotides once these polymers have undergone some degradation as a result either of heating or limited treatment with pancreatic DNase.
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A deoxyribonucleic acid phosphatase-exonuclease from escherichia coli. i. purification of the enzyme and characterization of the phosphatase activity.

TL;DR: The ability of this DNA phosphatase activity to remove the 3’-phosphoryl end groups of high molecular weight oligonucleotides provides a useful reagent for studying the effect of such end groups in the DNA-synthesizing system.
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