Fibrinogen “Zurich” Separation of a Pathological from a Normal Fibrin Fraction
1970
Publisher Summary This chapter describes unstable hemoglobin with a modified affinity for oxygen in a French patient. This hemoglobin has been found in three members of the same family and is accompanied by identical symptoms that include a moderate hemolytic anemia, slight reticulocytosis, and the presence of red cell inclusion bodies. Electrophoresis of this hemoglobin at pH 8.6 shows a somewhat diffuse band representing 10–15% of the total, migrating a little in front of hemoglobin A 2 . There is also a very slow constituent to be seen, which could be free α-chain. This hemoglobin is unstable. Different stability tests have been studied after the initial elimination of nonhem proteins. This hemoglobin is thermolabile and a seizable precipitate is also obtained by incubation in the presence of para-hydroxy-mercuribenzoate. Purification of the supplementary peak shows a peptide similar to βT5 in its composition but modified specifically by the absence of an aspartic residue and a proline residue
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