Open AccessThe Synthesis and Properties of the Sepharose‐Bound tRNA Nucleotidyltransferase
Author(s) -
Litvak Simon,
TarragoLitvak Laura,
Carre Danièle S.,
Chapeville François
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb19677.x
Subject(s) - sepharose , cyanogen bromide , biochemistry , chemistry , enzyme , trypsin , protease , transfer rna , peptide sequence , rna , gene
The synthesis of an insoluble tRNA nucleotidyltransferase by covalent coupling of the enzyme to cyanogen bromide‐activated sepharose is described. The sepharose‐bound enzyme is active in the repair of the pCpCpA sequence of tRNA. Most of its properties are identical to the soluble enzyme although its stability, regarding thermal inactivation and trypsin digestion, is increased. However, tRNA, which protects the soluble enzyme against thermal denaturation and protease digestion, surprisingly does not protect the sepharose‐bound enzyme.