Henioglobin Polymorphism in White-Tailed Deer: Subunit Basis

By H’ mit si KITCHEN, FRANK W . PUTNAM AND \V. JAPE TAYLOR I HE SICKLING OF ERYTHROCYTES under in vitro laboratory conditions has been demonstrated in most species of deer. This remarkable distortion of the erythrocytes from the biconcave disc shape to such bizarre forms as holly leaf, crescent and oat shapes in several species of deer was first described by Gulliver in 1840. Seventy years later Herrick2 independently observed the existence of similarly shaped erythrocytes associated with a severe anemia in man. In contrast to the racial and geographical prevalence of the sickled erythrocyte associated with sickle cell anemia in man, the sickling phenomenon occurs in most species of the deer which represent a variety of ecological and geographical areas of the world. Sickling in the deer is an in vitro phenomenon which occurs under high oxygen tension and elevated pH and has no apparent pathological consequences.3’4 However, the occurrence of polymorphic hemoglobins and their relationship to the sickling or nonsickling of erythrocytes has been reported only in white-tailed deer (Odocoileus virginianus).3 Although the predominant number of deer have erythrocytes which have the propensity to sickle, this ability to assume reversibly bizarre erythrocyte forms cannot be attributed to the presence of a particular hemoglobin common to all white-tailed deer. In white-tailed deer the various polymorphic hemoglobins occur so frequently in the population that it is difficult to identify individual components as “normal” or “variant.” Hemoglobin heterogeneity has been reported in many mammalian species other than man.5 However, in most cases only two or three hemoglobins are found within a species. The white-tailed deer, having seven adult and two fetal hemoglobins, is a marked exception. This study will establish that the hemoglobin heterogeneity of white-tailed deer is due to structural differences in the protein moieties and describes the subunit basis for these polymorphic hemoglobins.