By William J. Cook

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I t i s t h u s i m p o r t a n t how t h e d e t e r g e n t i s removed t o o b t a i n w a t e r - s o l u b l e a g g r e g a t e s o f t h e s e i n t e g r a l membrane p r o t e i n s . The l i p i d - and d e t e r g e n t - f r e e g l y c o p r o t e i n h a s a sedi^ mentation coefficient o f a b o u t 26 S a n d a m o l e c u l a r weight of about 900,000. The 26 S c o m p l e x h a s a s i m i l a r r o s e t t e - l i k e s t r u c t u r e a s t h e 23 S complex in the e l e c t r o n microscope ( F i g .

The only exception appears to be the toga virus group to which SFV belongs. In the myxo-, paramyxo- and rhabdovirus groups the polypeptide with the lowest molecular weight is a major nonglycosylated polypeptide (3). This protein is not present in the nucleocapsid, and is thought to be associated with the internal surface of the viral membrane. Several observations indicate that these polypeptides form a shell of protein beneath the lipid membrane. Whether these polypeptides interact with the hydrocarbon interior of the lipid membrane or wheth er they are more peripheral to the membrane struc ture is not known.

The inabil_ ity of the protease-released protein to form these aggregates could be due to the cleavage of hydrophobic peptide segments involved in attaching the spike glycoproteins to the membrane. It is therefore likely that an amphipathic structure may be a general characteristic of viral spike glycoproteins, and hydrophobic peptide segments similar to those found in the SFV glycoproteins should be searched for. Intestinal mzmbKam ptiot. Most enveloped viruses contain at least one non-glycosilated pro tein in addition to the proteins of the nucleocapsid.

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