Two different forms of aggregated dimers of ribonuclease A.
Results of gel filtration experiments performed with two different chromatographic media (Superose 12 HR 10/30 and Superdex 75 HR 10/30) and of polyacrylamide gel electrophoresis under non-denaturing and denaturing conditions suggest that aggregated dimers of bovine RNase A, obtained by lyophilization of the enzyme from 40% acetic acid solutions (5 mg RNase A per ml), might consist of two differently structured forms. These two species have slightly different retention times in gel-filtration experiments and migrate differently in electrophoresis under non-denaturing conditions. The fast migrating dimer in non-denaturing gel electrophoresis is able to degrade double-stranded poly(A).poly(U) more efficiently than the other, and the two forms are found in a ratio of about 3:1.
Dipartimento di Scienze Neurologiche e della Visione, Sezione di Chimica Biologica, Facoltà di Medicina e Chirurgia, Università di Verona, Strada Le Grazie 8, I-37134 Verona, Italy.
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Libonati
D002850:Chromatography, Gel; D003432:Cross-Linking Reagents; D019281:Dimerization; D004120:Dimethyl Suberimidate; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*
D003432:Cross-Linking Reagents; D004120:Dimethyl Suberimidate; D012259:Ribonuclease, Pancreatic