
%0 Journal Article
%A Dopheide, TAA 
%A Inglis, AS 
%T Primary Structure of Apovitellenin I From Hen Egg Yolk and its Comparison With Emu Apovitellenin I
%J Australian Journal of Biological Sciences
%D 1976/06/01
%V 29
%N 3
%P 175-180
%K 
%R https://doi.org/10.1071/BI9760175
%U https://www.publish.csiro.au/paper/BI9760175 
%X 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. 
