Synthesis of Non‐globin Proteins in Rabbit‐Erythroid Cells

Abstract

Peripheral rabbit reticulocytes synthesize at least 30 non-globin proteins. One is identified as a characteristic lipoxygenase (EC 1.13.11.12) on the basis of its MW, its immunological properties and its behavior 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 anemia, increases up to the 5th day and stays constant at least up to the 14th day. The appearance of the lipoxygenase, which plays a key role in the degradation of mitochondria in the course of maturation of reticulocytes to erythrocytes, is apparently regulated at the translational level.