A Two-Dimensional Peptide Gel Electrophoresis System for Phosphopeptide Mapping and Amino Acid Sequencing

1999 ◽  
Vol 266 (2) ◽  
pp. 198-204 ◽  
Author(s):  
Andrea Gatti ◽  
Jolinda A. Traugh
2012 ◽  
Vol 76 (3) ◽  
pp. 594-597 ◽  
Author(s):  
Takanari SHIGEMITSU ◽  
Yuhi SAITO ◽  
Shigeto MORITA ◽  
Shigeru SATOH ◽  
Takehiro MASUMURA

2010 ◽  
Vol 36 (4) ◽  
pp. 612-619 ◽  
Author(s):  
Lu GAN ◽  
Dian-Rong LI ◽  
Xin ZANG ◽  
Chun-Hua FU ◽  
Long-Jiang YU ◽  
...  

1985 ◽  
Vol 63 (8) ◽  
pp. 824-829
Author(s):  
C. C. Liew ◽  
Peter C. Hentzen ◽  
Isaac Bekhor

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.


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