|
|
||||||||
1 Department of Physiology, University of New England, Armidale, New South Wales, Australia
A new hemoglobin was produced in sheep with Hb A during experimental anemias. This hemoglobin, called Hb A
, had different electrophoretic characteristics and denatured with alkali at a faster rate than normal Hb A. It also showed electrophoretic differences to Hb B and Hb F. Hb A
was located almost entirely in the reticulocytes produced during the anemia. The reticulocytes produced in anemic sheep with Hb B contained a hemoglobin which showed only minor differences from the normal hemoglobin on electrophoresis. However, it denatured at a faster rate than the normal hemoglobin. It is postulated that Hb A
is a relatively unfinished hemoglobin associated with the immature erythrocytes produced after a severe anemic stress. It did not appear to be fetal hemoglobin.
Key Words: erythropoiesis hemoglobin types of sheep reticulocytes hypoxia
Submitted on December 11, 1964
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |