Synthesis of non-globin proteins in rabbit-erythroid cells. Synthesis of a lipoxygenase in reticulocytes.
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.
D000818:Animals; D001854:Bone Marrow Cells; D002454:Cell Differentiation; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004900:Erythroblasts / Q000201:enzymology; D066298:In Vitro Techniques; D008084:Lipoxygenase / Q000096:biosynthesis* / Q000097:blood; D011233:Precipitin Tests; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology*; D013997:Time Factors
D008084:Lipoxygenase