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

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.

scholarly journals Evidence for a phosphorylated form of calmodulin in chicken brain and muscle

1983 ◽  
Vol 3 (8) ◽  
pp. 1412-1420
Author(s):  
Y D Plancke ◽  
E Lazarides
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Amino Acid Analysis ◽  
Brain Slices ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Conventional Procedure ◽  
Phosphorylated Form ◽  
Acidic Proteins

Phosphocalmodulin (PCaM) was identified after analysis of calmodulin (CaM) preparations by two-dimensional gel electrophoresis by using a modified ampholyte system to resolve very acidic proteins. The analysis of CaM prepared by the conventional procedure based upon its heat resistance and acidity as well as the analysis of whole urea extracts from brain showed that PCaM was a major component in this tissue. PCaM was 1 pH unit more acidic than CaM, and its electrophoretic mobility, unlike CaM, was not changed by either calcium or ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid. In urea extracts of brain prepared in buffers containing phosphate and sodium fluoride, PCaM was as prominent as CaM; it was partially converted into CaM after elution from the gel and reelectrophoresis. Amino acid analysis of PCaM and CaM purified by two-dimensional gel electrophoresis showed the same composition for the two proteins, including their trimethyllysine content. Incorporation of 32P occurred exclusively into the acidic variant when brain slices were incubated with H332PO4; amino acid analysis showed that the phosphate was bound to serine residues. CaM was found also to be phosphorylated in vitro by a phosphorylase kinase preparation from skeletal muscle.

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