Electronic Resource
Springer
Molecular genetics and genomics
104 (1969), S. 157-164
ISSN:
1617-4623
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary Ribosomal proteins from rat liver were separated by chromatography on carboxymethyl-cellulose into 9 fractions, which differ significantly in their electrophoretic pattern on polyacrylamide gel. Two of the fractions are homogeneous on examination by electrophoresis, two others contain a main component and several weak bands. Another protein component was isolated by filtration of a chromatographic fraction on Biogel P 10. Amino acid composition, N-terminal amino acids and molecular weights of the proteins were determined. The combination of ion exchange chromatography and disc electrophoresis shows, that some chemically distinct proteins have almost identical electrophoretic mobility and other ones possess the same binding properties to CM-cellulose.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00272797
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