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Hemoglobin is a principal protein involving in respiration in most mamamals and their main function is to carry oxygen troughout the body. Insects have been of particular interests since they too use globin proteins, however the large majority. The authors in this paper describe early work using synthetic oligonucleotides in the isolation of globin genes from a Chironomus thummi cDNA bank. A strecht of 584 base pair sequence was found to encode the N-terminal hydrophobic signal sequence and also the full sequence of a mature secreted globin; a polyadenylation recognition site 3'''' to an appropriate stop codon, was also identified. The deduced amino acid sequence corresponds to an unreported variant of hemoglobin VIIB. According to the nucleotide differences between Hb VIIB chains, the pC-S9 gene cloned and sequence in this work one can say that it has been evolutionarily independent for a longer period of time than the other two known members of the globin VIIB lineage.
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