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This investigation reveals the AHF activity in the A-2 globulin region, highlighting its molecular characteristics and implications.
L ittle is known of the molecular size or structure of antihaemophilic factor (AHF)‐also known as Factor VIII or antihaemophilic globulin (AHG). It is generally assumed to be a protein and has been characterized electrophoretically as a B‐2 globulin (Spaet and Kinsell, 1953; van Creveld, Hoorweg, den Ottolander and Veder, 1956). Hardisty and Pinniger (1956) found that it migrated with the B‐globulin fraction. In the course of using the method of starch‐block electrophoresis for the separation of clotting factors from human plasma we have found the AHF activity in the a ‐2 globulin region, and have failed to detect similar activity in any of the B ‐globulin fractions. In this paper we report and discuss these findings.
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Barkhan et al. (1963) studied this question.
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