the cause of the alteration in properties. Another possible cause may be that the acid group liberated by the nuclease (1) concerns the adenine radical and that some other alteration in the nucleic acid molecule prevents the initial hydrolysis by the nuclease necessary for the eventual liberation of
Abstract of Effect of borate on a protein-polysaccharide complex, the phosphoesterase from calf intestinal mucosa : Charles A. Zittle (Journal of Biological Chemistry, 167: 297. 1947)
- Publisher
- Elsevier Science
- Year
- 1947
- Tongue
- English
- Weight
- 66 KB
- Volume
- 244
- Category
- Article
- ISSN
- 0016-0032
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โฆ Synopsis
in an attempt to fractionate a preparation of phosphodiesterase isolated from calf intestinal mucosa, borate was added prior to ammonium sulfate precipitation.. The solubility of the preparation was reduced by the addition of the borate and a polysaccharide-rich, enzyme-poor fraction could be precipitated by one-half saturation with ammonium sulfate. The enzyme fraction, which could be precipitated at a higher concentration of ammonium sulfate, was twice as active, on a unit weight basis, as the starting material. Phosphodiesterase activity and phosphomonoesterase (alkaline phosphatase) activity were reversibly inhibited approximately 50 per cent. by 0.01 M borate. The data suggest that the enzyme may be a protein-polysaccharide complex.
๐ SIMILAR VOLUMES
tempt to fractionate a preparation of phosphodiesterase isolated from calf intestinal mucosa, borate was added prior to ammonium sulfate precipitation.. The solubility of the preparation was reduced by the addition of the borate and a polysaccharide-rich, enzyme-poor fraction could be precipitated b