Abstract
Summary
Hemoglobin was prepared from adult pigs and from fetuses in the second month of gestation. Both the adult and fetal pig hemoglobin consisted of one major component on electrophoresis in barbital buffer at pH 8.6. However, the adult pig hemoglobin had a faster mobility under these electrophoretic conditions than did the fetal pig hemoglobin. On amino acid analysis, using the accelerated Moore and Stein column technique, it was found that both the fetal and adult pig hemoglobin had one isoleucine per dimer subunit. On alkaline denaturation, it was found that the adult pig hemoglobin denatured more slowly and to a lesser extent than did fetal pig hemoglobin. The adult pig hemoglobin had 32.1 ± 6.1% of the hemoglobin still undenatured at the end of 15 min, while fetal pig hemoglobin only had 16.8 ± 4.4% still undenatured. The peptide fingerprint pattern showed that less than half of the peptides had been altered when comparing adult and fetal hemoglobin. It is concluded that there are two distinct hemoglobins in the pig; an adult hemoglobin and a fetal hemoglobin.
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