Abstract:
:Ribosomal 60S subunits active in polyphenylalanine synthesis can be reconstituted from core particles lacking 20-40% of the total protein. These core particles were obtained by treatment of yeast 60S subunits with dimethylmaleic anhydride, a reagent for protein amino groups. Upon reconstitution a complementary amount of split proteins is incorporated into the ribosomal particles, which have the sedimentation coefficient of the original subunits. Ribosomal protein fractions obtained by extraction with 1.25 M NH4Cl, 4 M LiCl, 7 M LiCl, or 67% acetic acid, are much less efficient in the reconstitution of active subunits from these core particles than the corresponding released fraction prepared with dimethylmaleic anhydride. Attempts to reconstitute active subunits from protein-deficient particles obtained with 1.25 M NH4Cl plus different preparations of ribosomal proteins, including the fraction released with dimethylmaleic anhydride, were unsuccessful. Therefore, under our conditions, of the disassembly procedures assayed only dimethylmaleic anhydride allows partial reconstitution of active 60S subunits.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Vioque A,Palacián Edoi
10.1007/BF00231823subject
Has Abstractpub_date
1985-02-01 00:00:00pages
55-60issue
1eissn
0300-8177issn
1573-4919journal_volume
66pub_type
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