The amino acid sequence of apovitellenin I from hen egg yolk has been determined using both automatic and manual procedures; it comprises 82 residues. Hen apovitellenin shows considerable homology with emu apovitellenin I which contains 84 residues. Besides two deletions in the sequence, the hen protein differs in 28 positions from the emu protein; 26 of these positions may have arisen from single base changes. The changes are largely conservative ones, which suggest that the structure and function have been preserved despite extensive mutation.
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Dopheide et al. (1976) studied this question.
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