Separation of cytoplasmic ribosomal proteins of Microsporum canis

1987 ◽  
Vol 33 (4) ◽  
pp. 339-343 ◽  
Author(s):  
Valsan Mandiyan ◽  
G. Ramananda Rao
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Large Subunit ◽  
Polyacrylamide Gel Electrophoresis ◽  
Small Subunit ◽  
Polyacrylamide Gel ◽  
Microsporum Canis ◽  
Two Dimensional ◽  
Molecular Weights

The cytoplasmic ribosomal proteins of Microsporum canis were characterised in basic–acidic and basic–SDS two-dimensional polyacrylamide gel electrophoresis systems. The small subunit contained 28 proteins and the large subunit 38 proteins. The molecular weights of these proteins were in the range of 32 500 to 7600 and 48 000 to 11 000 in the small and large subunits, respectively. The 80S ribosomes showed 65 and 66 protein spots in basic–acidic and basic–SDS gel systems, respectively.

scholarly journals Reductive alkylation of ribosomes as a probe to the topography of ribosomal proteins*

1974 ◽  
Vol 143 (3) ◽  
pp. 607-612 ◽  
Author(s):  
Graham Moore ◽  
Robert R. Crichton
Keyword(s):  
Escherichia Coli ◽  
Protein Complex ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Reductive Alkylation ◽  
Lysine Residues

Escherichia coli ribosomes were treated with a number of different aldehydes of various sizes in the presence of NaBH4. After incorporation of either 3H or 14C, the ribosomal proteins were separated by two-dimensional polyacrylamide-gel electrophoresis and the extent of alkylation of the lysine residues in each protein was measured. The same pattern of alkylation was observed with the four reagents used, namely formaldehyde, acetone, benzaldehyde and 3,4,5-trimethoxybenzaldehyde. Every protein in 30S and 50S subunits was modified, although there was considerable variation in the degree of alkylation of individual proteins. A topographical classification of ribosomal proteins is presented, based on the degree of exposure of lysine residues. The data indicate that every protein of the ribosome has at least one lysine residue exposed at or near the surface of the ribonucleo-protein complex.

scholarly journals Quantitation of eukaryotic ribosomal proteins separated by two-dimensional polyacrylamide gel electrophoresis

FEBS Letters ◽  
1975 ◽  
Vol 56 (2) ◽  
pp. 205-211 ◽  
Author(s):  
O.H.W. Martini ◽  
Richard Temkin ◽  
Alwyn Jones ◽  
Kate Riley ◽  
H.J. Gould
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional
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