The primary structure of rat liver ribosomal protein L39.

A Lin,J Mcnally,I G Wool

doi:10.1016/s0021-9258(17)43687-8

Abstract

The covalent structure of the rat liver 60 S ribosomal subunit protein L39 was determined. Fourteen tryptic peptides were purified, and the sequence of each was established by a micromanual procedure; they accounted for all 50 residues of L39. The sequence of the NH2-terminal 32 residues of L39, obtained by automated Edman degradation of the intact protein, provided the alignment of the first seven tryptic peptides. Two peptides, CNI (28 residues) and CNII (22 residues), were produced by cleavage of protein L39 with cyanogen bromide and the sequence of CNII was determined by automated Edman degradation. This sequence established the order of tryptic peptides T8 through T14. The carboxyl-terminal amino acids were identified after carboxypeptidase A treatment. Protein L39 contains 50 amino acids and has a molecular weight of 7308. There are indications that a portion of rat L39 is related to a fragment of Escherichia coli ribosomal protein S1.

Highlights

The covalent structure of therat liver 60 S ribosomal sequence of a cyanogen bromidefragment (Fig. 4).The amino subunit protein L39 wasdetermined
CNI (28 residues) and CNII (22 residues), were produced by cleavage of protein L39 with cyanogen bromide and the sequence of CNII was determined by automated Edman degradation
Protein L39 is rich in basic amino acids (9 lysyl, 9 arginyl, and 2 histidyl residues), contains no acidic amino acids, and lacksvaline and cysteine

Summary

Introduction

The covalent structure of therat liver 60 S ribosomal sequence of a cyanogen bromidefragment (Fig. 4).The amino subunit protein L39 wasdetermined. Protein L39 contains 50 amino acids and has a molecular weight of 7308. There are indications that a portion of rat L39 is related to a fragment of Escherichia coli

Results

Conclusion