Ovalbumin utilizes an NH2-terminal signal sequence.

In synchronized translation experiments in the wheat germ and reticulocyte lysate systems, ovalbumin (385 amino acids) was glycosylated by and segregated in dog pancreatic microsomes only if microsomes were added before the nascent ovalbumin polypeptide contained less than 150 amino acids. This would place the "signal" sequence of ovalbumin prior to residue 150, in contrast to a previous report.