Complete amino acid sequence of human phosphoglycerate kinase. Isolation and amino acid sequence of tryptic peptides.

I.Y Huang,E Rubinfien,A Yoshida

doi:10.1016/s0021-9258(18)43753-2

Abstract

As a part of the elucidation of the complete amino acid sequence of human phosphoglycerate kinase, 46 tryptic peptides, ranging in length from 1 to 26 residues, were isolated and characterized from the reduced and S-carboxymethylated enzyme. The isolated peptides were subjected to sequence analysis by the modified dansyl-Edman degradation procedure and automated Edman degradation technique. The results, together with the data on cyanogen bromide peptides and two additional tryptic peptides from cyanogen bromide peptides reported in the accompanying paper, established the complete amino acid sequence of human erythrocyte phosphoglycerate kinase.

Highlights

Acid sequence of human phosphoglycerate kinase, 46 tryptic peptides, ranging in length 1ftroo2m6 residues, were isolated and characterized from the reduceadnd
S-carboxymethylatedenzyme.Theisolatedpeptides were subjected to sequence analysis by the modified dansyl-Edman degradation procedure and automated Edman degradationtechnique.The results, together with the data on cyanogen bromide peptides and two additionaltrypticpeptidesfromcyanogenbromide peptides reported in the accompanying paper, estab
Human phosphoglycerate kinase in erythrocytes and other tissues, except for terminal amino acid of each peptide when it waspurified by two-dimensional paper electrophoresis and paper chromatography, located by spraying with fluorescamine, and eluting with 2 M acetic acid

Summary

Introduction

Acid sequence of human phosphoglycerate kinase, 46 tryptic peptides, ranging in length 1ftroo2m6 residues, were isolated and characterized from the reduceadnd. As a part of the elucidation of the complete amino acid sequence of human phosphoglycerate kinase, 46 tryptic peptides, ranging in length 1ftroo2m6 residues, were isolated and characterized from the reduceadnd S-carboxymethylatedenzyme.Theisolatedpeptides were subjected to sequence analysis by the modified dansyl-Edman degradation procedure and automated Edman degradationtechnique.The results, together with the data on cyanogen bromide peptides and two additionaltrypticpeptidesfromcyanogenbromide peptides reported in the accompanying paper, estab-

Results

Conclusion