Nonreducing two-dimensional polyacrylamide gel electrophoretic analysis of human colonic proteins

1995 ◽  
Vol 16 (1) ◽  
pp. 1120-1130 ◽  
Author(s):  
Gavin E. Reid ◽  
Hong Ji ◽  
James S. Eddes ◽  
Robert L. Moritz ◽  
Richard J. Simpson
Keyword(s):  
Electrophoretic Analysis ◽  
Polyacrylamide Gel ◽  
Two Dimensional

scholarly journals Cell-surface discoidin in aggregating cells of Dictyostelium discoideum

1982 ◽  
Vol 204 (3) ◽  
pp. 787-794 ◽  
Author(s):  
I C Madley ◽  
M J Cook ◽  
B D Hames
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Dictyostelium Discoideum ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Electrophoretic Analysis ◽  
Integral Membrane Protein ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Surface Receptors

Both discoidin I and discoidin II have been detected on the surface of aggregating (10 h developmental stage) cells of Dictyostelium discoideum NC4 by radioiodination of the cell-surface followed by immunoprecipitation and sodium dodecyl sulphate/polyacrylamide-gel-electrophoretic analysis. Approx. 92% of cell-surface discoidin I and 72% of cell-surface discoidin II can be eluted with 0.5 M-galactose, showing that most of each endogenous lectin is not present as integral membrane protein but rather is bound to cell-surface discoidin receptors. Two-dimensional polyacrylamide-gel-electrophoretic analysis of discoidin I suggests that the native tetramer may be a hetero-multimer composed of both Ia and Ib subunits. Cell-surface discoidin I also contains both types of subunit, but it is not clear whether both subunits have corresponding cell-surface receptors.

scholarly journals Modification of yeast ribosomal proteins. Methylation

1978 ◽  
Vol 175 (1) ◽  
pp. 221-225 ◽  
Author(s):  
T Kruiswijk ◽  
A Kunst ◽  
R J Planta ◽  
W H Mager
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Electrophoretic Analysis ◽  
Polyacrylamide Gel ◽  
Methyl Groups ◽  
Two Dimensional ◽  
Protein Species ◽  
Methyl Group

Two-dimensional polyacrylamide-gel electrophoretic analysis of yeast ribosomal proteins uniformly labelled in vivo with [methyl-3H]methionine and [1-14C]methionine revealed that four ribosomal proteins are methylated, i.e. proteins S31, S32, L15 and L41. Lysine and arginine appear to be the predominant acceptors of the methyl groups. The degree of methylation ranges from 0.09 to 0.20 methyl group per modified ribosomal protein species.

Fractionation of nucleoli. Enzymic and two-dimensional polyacrylamide gel electrophoretic analysis

Biochemistry ◽  
1977 ◽  
Vol 16 (21) ◽  
pp. 4716-4721 ◽  
Author(s):  
Lawrence I. Rothblum ◽  
Paula M. Mamrack ◽  
H. M. Kunkle ◽  
Mark O. J. Olson ◽  
Harris Busch
Keyword(s):  
Electrophoretic Analysis ◽  
Polyacrylamide Gel ◽  
Two Dimensional
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