
TY  - JOUR
A1  - Dopheide, TAA 
A1  - Inglis, AS 
T1  - The Amino Acid Sequence of a Protein (Apovitellenin I) From the Low-density Lipoprotein of Emu Egg Yolk
JF  - Australian Journal of Biological Sciences
JO  - Aust. Jnl. Of Bio. Sci.
Y1  - 1974
VL  - 27
IS  - 1
SP  - 15
EP  - 22
KW  - 
UR  - https://doi.org/10.1071/BI9740015 
N2  - The amino acid sequence of apovitellenin I from emu (Dromaius novae-hollandiae) egg yolk has been determined. Difficulties were encountered during sequencing, due to a labile Tyr-Val bond, which was hydrolysed readily by trypsin, chymotrypsin and pepsin. By use of a sequenator, this bond was easily characterized. The protein contains 84 residues and is devoid of half-cystine and histidine. Hydrophobic residues occur in clusters; two very hydrophobic sequences of 12 and 13 residues are present. A very hydrophilic sequence of seven residues contains nearly one-third of all side-chain charges in the molecule; the remainder of the polar residues are scattered throughout the sequence. In a number of instances, residues with opposite charges occur in adjacent positions. 
ER  -

