Isolation and Characterization of Two Hemoglobins Found in the Turtle, Pseudemys scripta elegans.

Abstract

Hemolysates of Pseudemys red cells contain 2 hemoglobins. These were isolated in either borate or barbiturate buffers, pH 8.6, ionic strength 0.01 or 0.05, with a Karler-Misco continuous flow electrophoretic unit (Microchemi-cal Specialties Co., Pasadena, California). The fastest migrating hemoglobin (Fast Hb) comprises 1/3 of total hemoglobin of the hemolysate. Isolated Fast Hb and the other component (Slow Hb) are homogeneous and bind O2 in a 11 molar ratio with respect to their Fe content. Fast Hb denatures in alkali almost as rapidly as human Hb A, has an iso-electric pH of 5.7 and a sedimentation constant of 4.6 svedbergs. Slow Hb is relatively stable in alkali, has an isoelectric pH of 7.2 and a sedimentation constant of 0.9 svedbergs. Electrophoretic mobilities of Slow Hb and Fast Hb in mixtures are different from the mobilities of the pure hemoglobins. Mobilities of Fast Hb and human Hb A in mixtures are identical with the mobilities of the pure hemoglobins. Data indicate the presence of an somewhat specific interaction between the turtle hemoglobins.