The purification and properties of a ribonuclease from squid

The purification and properties of a ribonuclease from squid

A ribonuclease in squid caecal fluid was partially purified and its properties studied. The enzyme is optimally active at pH 5.3 and is relatively stable to heating and treatment with acid. It was purified approximately 300-fold by heat treatment and salt gradient elution from a carboxymethylcellulo...

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Veröffentlicht in:Archives of biochemistry and biophysics 1960-08, Vol.89 (2), p.207-212
Hauptverfasser: Edmonds, Mary, Roth, Jay S.
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Sprache:eng
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Animals
Decapodiformes
Mollusca - chemistry
Old Medline
Ribonucleases - chemistry
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Roth, Jay S.
description A ribonuclease in squid caecal fluid was partially purified and its properties studied. The enzyme is optimally active at pH 5.3 and is relatively stable to heating and treatment with acid. It was purified approximately 300-fold by heat treatment and salt gradient elution from a carboxymethylcellulose column. The purified enzyme was free of deoxyribonuclease, phosphatase, and phosphodiesterase activity. Specificity studies indicated that the squid enzyme could hydrolyze either purine or pyrimidine diester bonds. It also slowly split, 2′,3′-cyclic adenosine phosphate but did not hydrolyze 2′,3′-cyclic pyrimidine phosphates.
doi_str_mv 10.1016/0003-9861(60)90044-8
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subjects Animals
Decapodiformes
Mollusca - chemistry
Old Medline
Ribonucleases - chemistry
title The purification and properties of a ribonuclease from squid
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