Abstract of hydrolysis of ribonucleic acid with phosphoesterase from calf intestinal mucosa: Charles A. Zittle (Journal of Biological Chemistry, 166:491, 1946)

• Publisher: Elsevier Science
• Year: 1947
• Tongue: English
• Weight: 70 KB
• Volume: 243
• Category: Article
• ISSN: 0016-0032
• DOI: 10.1016/0016-0032(47)90155-5

✦ Synopsis

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 adenosine by the phosphoesterase.

The inability of the nuclease to act on the alkali-treated (deaminated?) nucleic acid suggests that the bond specifically broken by this enzyme may involve the adenine group. Since the adenine group is also in ribonucleic acid, all of the bonds of which are hydrolyzed by phosphoesterase (4), a different bonding is suggested for the nucleotide containing this group in desoxyribonucleic acid. Desoxyribonucleic acid deaminated by the use of nitrite, which has been used to deaminate ribonucleic acid (5), would be of interest in this connection. This deamination procedure would probably not degrade the nucleid acid molecule to the degree that alkali does.

SUMMARY.

Desoxyribonucleic acid prepared by a method which utilizes strong NaOH was not acted on by a specific nuclease but it was extensively hydrolyzed by phosphoesterase from calf intestinal mucosa. Experiments indicated that the adenine radical is concerned in the resistance of the nucleic acid to the nuclease.