Abstract:
:Trypsin immobilized on collagen membranes has been used to digest accessible ribosomal proteins of rat liver 40 S subunits. Six proteins (S2, S6, S10, S14, S15 and S25) have been found to be highly exposed on the surface of 40 S particles. They appear to be in close physical contact and localized in the same region of the subunit, most likely protruding at its surface. Electric birefringence reveals that digestion of these proteins results in unfolding of subunits: the birefringence of 40 S particles becomes negative, like that of RNA, the relaxation time undergoes a 15-fold decrease and the mechanism of orientation is drastically modified.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Marion MJ,Marion Cdoi
10.1016/0014-5793(88)80753-1subject
Has Abstractpub_date
1988-05-23 00:00:00pages
281-5issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(88)80753-1journal_volume
232pub_type
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