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Microscale electrophoresis of stress proteins induced by chemicals during the in vivo cell cycle
Author(s) -
Pipkin James L.,
Anson Jeanne F.,
Hinson William G.,
Robert Burns E.,
Casciano Daniel A.
Publication year - 1986
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150071007
Subject(s) - chemistry , sodium arsenite , leucine , sodium , gel electrophoresis , biochemistry , phosphate , polyacrylamide gel electrophoresis , chromatography , amino acid , enzyme , arsenic , organic chemistry
The incorporation of leucine and phosphate in proteins extracted with two different solvents from nuclei sorted physically from the G 0 +G 1 phase of the rat submaxillary gland cell cycle was observed by two‐dimensional microscale polyacrylamide gel electrophoresis. Sodium phenobarbital did not initiate additional isotope ([ 3 H]leucine and [ 32 P]phosphate) incorporation on its own. After dosing with DL ‐isoproterenol, several proteins incorporated leucine and phosphate during the G 0 +G 1 phase. The inclusion of phenobarbital in the dosing regime enhanced labeling of several proteins already present in the G 0 +G 1 phase. Treatment of animals with sodium arsenite prompted labeling of phosphate of two “stress” proteins in the non‐dividing G 0 phase of the submaxillary gland. Enhanced incorporation of proteins was exhibited after combined dosing of isoproterenol and sodium arsenite, but no new incorporated proteins were seen in the G 0 +G 1 phase. Likewise, no new proteins were seen to incorporate in the G 2 +M phase, but there was some increased incorporation in a few already present proteins under these conditions. The similar mobilities of several stress proteins, which were determined by coelectrophoresis of stress marker proteins, suggested that several of these proteins, even though they were extracted with different solvents, were identical.