Comparison of14C-amino acid mixture and [35S]methionine labeling of cellular proteins from mouse fibroblast C3H10T1/2 cells by two-dimensional gel electrophoresis

1991 ◽  
Vol 12 (9) ◽  
pp. 658-666 ◽  
Author(s):  
Chaoying He ◽  
B. Alex Merrick ◽  
Betty K. Mansfield ◽  
M. Catherine Hite ◽  
Dennis R. Daluge ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Amino Acid Mixture ◽  
Mouse Fibroblast ◽  
Cellular Proteins ◽  
Acid Mixture ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Separation and Identification of Rice Prolamins by Two-Dimensional Gel Electrophoresis and Amino Acid Sequencing

2012 ◽  
Vol 76 (3) ◽  
pp. 594-597 ◽  
Author(s):  
Takanari SHIGEMITSU ◽  
Yuhi SAITO ◽  
Shigeto MORITA ◽  
Shigeru SATOH ◽  
Takehiro MASUMURA
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Amino Acid Sequencing ◽  
Two Dimensional Gel Electrophoresis

scholarly journals Response of poly(adenylic acid) polymerase in rat liver nuclei and mitochondria to starvation and re-feeding with amino acids

1976 ◽  
Vol 158 (2) ◽  
pp. 161-167 ◽  
Author(s):  
S T Jacob ◽  
K M Rose ◽  
H N Munro
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Protein Content ◽  
Total Activity ◽  
Amino Acid Mixture ◽  
Cellular Proteins ◽  
Acid Mixture ◽  
Total Protein Content ◽  
Adenylic Acid ◽  
Liver Nuclei

Poly(adenylic acid) polymerase was extracted from liver nuclei and mitochondria of rats either fed ad libitum, starved overnight or starved and then re-fed with a complete amino acid mixture for 1-3 h. The enzymes were partially purified and assayed by using exogenous primers. Starvation resulted in an 80% decrease in the total activity of the purified nuclear enzyme, and the mitochondrial enzyme activity diminished to almost zero after overnight starvation. Measurements of the protein content of whole nuclei or mitochondria and of the enzyme extracts from these organelles indicated that the decrease in enzyme activity on starvation was not caused by incomplete extraction of the enzyme from the starved animals. Re-feeding the animals with the complete amino acid mixture increased the total activity of poly(A) polymerase from the nuclei and mitochondria by 1.9-fold and 63-fold respectively. Under these conditions, the total protein content of the nuclei and mitochondria increased by only 13 and 32% respectively. These data indicate that poly(A) polymerase is one of the cellular proteins specifically regulated by amino acid supply.

Partial characterization of chromosomal proteins tightly bound to chicken erythroid DNA

1985 ◽  
Vol 63 (8) ◽  
pp. 824-829
Author(s):  
C. C. Liew ◽  
Peter C. Hentzen ◽  
Isaac Bekhor
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Basic Amino Acid ◽  
Two Dimensional ◽  
Amino Acid Residues ◽  
Two Dimensional Gel Electrophoresis ◽  
Total Dna ◽  
Chromatin Proteins

Extraction of chicken reticulocyte and erythrocyte chromatins with 2 M NaCl yields a small fraction (about 5%) of the total DNA which is very tightly bound to a class of nonhistone chromatin proteins (DNA–P). This DNA fraction has previously been shown to be significantly enriched in active gene sequences. The proteins associated with reticulocyte and erythrocyte DNA–P were analyzed by two-dimensional gel electrophoresis. Reticulocyte DNA–P yield predominantly three major proteins, designated G1, G2, and G3 with relative masses of 80 000, 50 000, and 58 000, respectively. Erythrocyte DNA–P show only two proteins which appear to be similar to the reticulocyte G1 and G2 proteins, except in much reduced quantities as revealed by two-dimensional polyacrylamide gel electrophoresis. Amino acid analysis of the three reticulocyte proteins revealed that the ratio of acidic to basic amino acid residues increased in the order G1 < G2 < G3, while the respective isoelectric points also increased in that order.

Sign in / Sign up

Export Citation Format

Share Document