Anomalous behavior or ribonuclease A on Sephadex G-100.
Ribonuclease A was found to behave in an unusual fashion on a Sephadex gel column. Though ribonuclease A produces a single, well-defined protein peak on elution, enzyme activity can be detected several void volumes after the protein peak. A second unrelated protein added to the column will displace further activity as will 0.5 M phosphate buffer. This additional activity, apparently due to ribonuclease A or an active fragment of the enzyme, would appear to make this enzyme unsuitable for use as a standard in molecular weight determinations of other nucleases.
Mitch
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Laboratory of Pharmacology, Baltimore Cancer Research Center, National Cancer Institute, National Institute of Health, 3100 Wyman Park Drive, Baltimore, Md. 21211, USA.
Levy
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D001419:Bacteria / Q000201:enzymology; D002850:Chromatography, Gel / Q000379:methods; D002919:Chymotrypsinogen; D003911:Dextrans; D005782:Gels; D007700:Kinetics; D008970:Molecular Weight; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D012260:Ribonucleases / Q000737:chemistry / Q000302:isolation & purification
D003911:Dextrans; D005782:Gels; C025614:sephadex; D002919:Chymotrypsinogen; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic