Hemoglobins, XXI: sequence analysis of porcine hemoglobin (author's transl)

The hemoglobin of a bavarian domestic pig (Suidae) was isolated. The chains were separated by countercurrent distribution, then cleaved with trypsin. The isolated peptides were sequenced with hydrophilic phenylisothiocyanate I and IV, or with a dimethylaminopropyne program in the sequenator. The sequences of the chains are given. Some methodical aspects of automatic sequencing are discussed and the sequences of human porcine hemoglobin are compared. The role of adult pig haemoglobin as foetal hemoglobin is discussed.     

Hemoglobins, XXXIV. "Hemoglobin Heide", a new embryonal hemoglobin. N-terminal sequence of the theta-chains (author's transl)

A new embryonic hemoglobin is described. Erythrocytes of pig embryos were lysed. The lysate was analyzed by gel-electrophoresis and the hemoglobins were separated on DEAE-Sephacel. The hemoglobin fractions were characterized by sequence analysis. We found in addition a new hemoglobin chain--theta-chain--not yet described. The primary structure of the theta-chains is similar to that of the epsilon-chains. There are only 3 differences in the first 30 residues. Furthermore, these theta-chains were found to be associated with theta-like chains and therefore we propose a hemoglobin of the type x2/theta 2 and we suggest the name "Hemoglobin Heide" for this new embryonic hemoglobin. In conclusion, four different globin gens (alpha-, epsilon-, theta- and theta-gens) and three different hemoglobins (Gower I, Gower II and Hb Heide) were detected in the embryonic respiration of mammals.     

Hemoglobins, XXX. The amino acid sequence of the monomeric hemoglobin from Lampetra fluviatilis (author's transl)]

The primary structure of the two main hemoglobin components of the river lamprey Lampetra fluviatilis was established. Having a chain length of 149 amino acids the molecular weight of the globin is 16272. The two main components differ only by an N-formyl residue at the N-terminal proline. The sequence was compared with those of two related species. The heterogeneity of Cyclostomata hemoglobins and their possible origin was discussed.