D-3-phosphoglycerate dehydrogenase fromEscherichia coli: isolation by affinity chromatography and sequence comparison to other dehydrogenases

Gregory A. Grant, Maria L. Zapp
1981 Bioscience Reports  
Escherichia coli D-3-phosphoglycerate dehydrogenase has been isolated in homogeneous form by a simple procedure employing 5'-AMP-Sepharose as an affinity adsorbent. The enzyme is composed of four identical polypeptide chains each with a molecular weight of approximately 40 000. Amino-terminal sequence analysis of the first 36 residues clearly establishes the relationship of this enzyme to other NAD-dependent dehydrogenases.
doi:10.1007/bf01116472 pmid:7049261 fatcat:lkyygu4yrzgftahuibuzhrizzm