GILLCHR1EST AND BOCK 



TABLE 1. Analysis of Nucleic Acid Hydrolyzed with 0.5 AT NaOH 



for 16 Hours at 37° C 



Hydrolyzate was chromatographed on a Dowex-1-formate column 

 with gradient elution. 



tates re-evaluation of some studies [10] that have been carried out on A. vine- 

 landii and raises the important question whether this phenomenon can occur 

 in ribonucleoprotein from other sources. 



The ribonucleoprotein has been assayed for a large number of enzymatic 

 activities. It appears free of nucleotide phosphatase activity, glucose-1-phos- 

 phatase, oxidative phosphorylation enzymes, and electron-transport enzymes. 

 A feeble glucose-6-phosphatase activity of 10 mM phosphate released per minute 



4900g SUPERNATE 



i\ 



t — J 



STANDARD 



F4 



SALT 



M 



RNASE 



-i 



EDTA 



DNASE 



Fig. 4. The preparation and stability of A. vinelandii nucleoprotein. Each analytical 

 ultracentrifuge pattern is labeled with the stage of preparation (top pair) or the treatment 

 to which a pure 86 S product was subjected. The salt and EDTA treatment are described 

 in the text. The RNAse action occurred in less than 5 minutes at 1 part of enzyme per 

 1000 parts of particle whereas the DNAse at the same concentration produced no change 

 in 45 minutes. 



