Open AccessSynthesis of Non‐globin Proteins in Rabbit‐Erythroid Cells
Author(s) -
THIELE Bernd J.,
BELKNER Jutta,
ANDREE Hartwig,
RAPOPORT Samuel M.,
RAPOPORT Tom A.
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb13070.x
Subject(s) - globin , mitochondrion , bone marrow , peripheral blood , hemoglobin , chemistry , lipoxygenase , biochemistry , enzyme , biology , microbiology and biotechnology , immunology
Peripheral rabbit reticulocytes synthesize at least 30 non‐globin proteins. One of them is identified as a characteristic lipoxygenase on the basis of its molecular weight, its immunological properties and its behaviour on an ion‐exchange column. The enzyme is not produced in bone marrow cells. The synthesis of the lipoxygenase in peripheral blood cells commences on the 3rd day of a bleeding anaemia, increases up to the 5th day and stays constant thereafter at least up to the 14th day. It is concluded that the appearence of the lipoxygenase, which plays a key role in the degradation of mitochondria in the course of maturation of reticulocytes to erythrocytes, is regulated at the translational level.