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Using one-and two-dimensional electrophoresis, the free and polyribosomal informosome proteins and a preparation of total RNA-binding proteins from rabbit reticulocytes were compared. It was shown that the major proteins of free and polyribosomal informosomes are similar only to the minor components of RNA-binding proteins. On the other hand, the major RNA-binding proteins, two of which are elongation translation factors EF-1L and EF2, can be present in informosome preparations only as minor components. The major proteins of polyribosomal informosomes do not coincide in terms of electrophoretic mobility with initiation factors eIF-2, eIF-2A, eIF-3, eIF-4A and eIF-4B. The major proteins of free informosomes differ in their electrophoretic mobility from initiation factors eIF-2A, eIF-4A and eIF-4B as well as from the alpha- and beta-subunits of initiation factor eIF-2.
V B Minich, and
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L P Ovchinnikov
June 1977,
Doklady Akademii nauk SSSR,
V B Minich, and
V I Klimyk, and
L P Ovchinnikov
April 1978,
FEBS letters,
V B Minich, and
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L P Ovchinnikov
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V B Minich, and
V I Klimyk, and
L P Ovchinnikov
October 1978,
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V B Minich, and
V I Klimyk, and
L P Ovchinnikov
October 1978,
European journal of biochemistry,
V B Minich, and
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L P Ovchinnikov
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Annual review of microbiology,
V B Minich, and
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L P Ovchinnikov
April 1976,
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V B Minich, and
V I Klimyk, and
L P Ovchinnikov
January 1979,
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V B Minich, and
V I Klimyk, and
L P Ovchinnikov
November 2013,
International journal of molecular sciences,
V B Minich, and
V I Klimyk, and
L P Ovchinnikov
February 2016,
Seikagaku. The Journal of Japanese Biochemical Society,
