scholarly journals Enzymic Adenosine Diphosphate Ribosylation of Histone and Poly Adenosine Diphosphate Ribose Synthesis in Rat Liver Nuclei

1968 ◽  
Vol 243 (13) ◽  
pp. 3765-3767 ◽  
Author(s):  
Y Nishizuka ◽  
K Ueda ◽  
T Honjo ◽  
O Hayaishi
Keyword(s):  
Rat Liver ◽  
Adenosine Diphosphate ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

scholarly journals The synthesis of nicotinamide–adenine dinucleotide and poly(adenosine diphosphate ribose) in various classes of rat liver nuclei

1969 ◽  
Vol 115 (5) ◽  
pp. 881-887 ◽  
Author(s):  
M E Haines ◽  
I R Johnston ◽  
A P Mathias ◽  
D. Ridge
Keyword(s):  
Dna Synthesis ◽  
Rat Liver ◽  
Nicotinamide Adenine Dinucleotide ◽  
Adenosine Diphosphate ◽  
Nicotinamide Adenine ◽  
Nad Metabolism ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Specific Activities

1. The activities of NMN adenylyltransferase and an enzyme that synthesizes poly (ADP-ribose) from NAD were investigated in the various classes of rat liver nuclei fractionated by zonal centrifugation. 2. The highest specific activities of these two nuclear enzymes occur in different classes of nuclei. In very young and in mature rats it was shown that a correlation exists between DNA synthesis and NMN adenylyltransferase activity, but in rats of intermediate age this correlation is less evident. The highest activities of the enzyme that catalyses formation of poly (ADP-ribose) are in the nuclei involved in the synthesis of RNA. 3. The significance of these results in relation to NAD metabolism is discussed.

scholarly journals Adenosine diphosphate ribosylated histones

1977 ◽  
Vol 161 (3) ◽  
pp. 583-592 ◽  
Author(s):  
M G Ord ◽  
L A Stocken
Keyword(s):  
Acid Hydrolysis ◽  
Rat Liver ◽  
Leucine Aminopeptidase ◽  
Adenosine Diphosphate ◽  
Histone Proteins ◽  
Rat Liver Nuclei ◽  
Histone 3 ◽  
Liver Nuclei ◽  
Serine Phosphate

When rat liver nuclei were incubated with [adenine-3H]NAD, besides histone 1, histone 2A and especially histone 2B accepted 3H radioactivity. 3H radioactivity was also found on the non-histone proteins and on the small amounts of histones 1 and 3 released into the supernatant during incubation. [14C]Adenine uptake in vivo by liver and thymus nuclei showed radioactivity in histones 1 and 3. After digestion with Pronase and leucine aminopeptidase 14C- or 32P-labelled histone 3 released a serine phosphate-containing nucleotide, which on acid hydrolysis yielded ADP-ribose and serine phosphate. Serine phosphate was also found in the material from the nucleotide peaks from histones 2A and 2B. ADP-ribosylated histones 1 and 3 were more easily released from nuclei than their unmodified forms and showed higher [32P]Pi and [3H]lysine uptakes in vivo [Ord & Stocken (1975) FEBS Meet. Proc. 34, 113-125].

scholarly journals Modulation by Exogenous Histones of Phosphorylation of Non-Histone Nuclear Proteins in Isolated Rat Liver Nuclei

1973 ◽  
Vol 248 (21) ◽  
pp. 7595-7600
Author(s):  
Edward M. Johnson ◽  
Giorgio Vidali ◽  
Virginia C. Littau ◽  
Vincent G. Allfrey
Keyword(s):  
Rat Liver ◽  
Nuclear Proteins ◽  
Isolated Rat Liver ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Isolated Rat
Sign in / Sign up

Export Citation Format

Share Document