Abstract
Two high mol. wt proteins have been identified and purified from newly laid eggs of Carausius morosus. Due to their apparent role in yolk formation, both proteins are taken to be vitellins, hereafter termed vitellin A and B. Upon dissociation by sodium dodecyl sulphate, vitellin A is shown to release two polypeptide subunits in equimolar ratio with a mol. wt of 180,000 and 70,000. When subjected to the same treatment, vitellin B releases three polypeptide subunits which range in mol. wt from 120,000 to 60,000. Antisera prepared against vitellins A and B show no sign of cross reaction with each other's antigen, whereas both react with haemolymph from adult females. Partial proteolysis of sodium dodecyl sulphate treated polypeptides reveals a number of electrophoretically similar low mol. wt fragments between the two. A model for the two egg proteins is proposed on the basis of the evidence available.
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