Abstract
A Triton X-100 acid urea gel system that gives a 2.5- to 3-cm separation of the rabbit globin peaks after 2 h of electrophoresis is described. The relative insensitivity of this method to large amounts of added protein allows a rapid analysis of low specific activity rabbit globins in various cell-free systems (rabbit reticulocyte lysate, wheat germ, duck reticulocyte lysate). These conditions give a similar separation for the globins of several other species. A 3.5-h electrophoresis under these conditions separates all the globin chains of human umbilical cord blood and allows the detection of the altered globin synthetic ratio of α-thalassemia-1 in small samples of cord blood.
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