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Amino acid sequence of the carboxy-terminal end of human erythrocyte glucose-6-phosphate dehydrogenase.
Human erythrocyte glucose-6-phosphate dehydrogenase was purified to homogeneity by a simplified procedure, consisting of 2',5'-ADP-Sepharose affinity chromatography, followed by Sephadex G-100 gel filtration. The carboxy-terminal region of the protein was identified by carboxypeptidase digestion: the sequence -Lys-Leu-COOH was found instead of the reported -Gly-COOH, thus showing identity with the carboxy-terminal sequence of glucose-6-phosphate dehydrogenase from human leukocytes and platelets. In addition, the carboxyl-terminal peptide was isolated from a tryptic digest of the protein and sequenced. The sequence is: Trp-Val-Asp-Pro-His-Lys-Leu.
PMID: 6696761 [PubMed - indexed for MEDLINE]
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Cited by 2 PubMed Central articles
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Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones: primary structure of the protein and unusual 5' non-coding region.
Persico MG, Viglietto G, Martini G, Toniolo D, Paonessa G, Moscatelli C, Dono R, Vulliamy T, Luzzatto L, D'Urso M.
Nucleic Acids Res. 1986 Mar 25; 14(6):2511-22.
[Nucleic Acids Res. 1986]
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Molecular diversity of glucose-6-phosphate dehydrogenase: rat enzyme structure identifies NH2-terminal segment, shows initiation from sites nonequivalent in different organisms, and establishes otherwise extensive sequence conservation.
Jeffery J, Söderling-Barros J, Murray LA, Hansen RJ, Szepesi B, Jörnvall H.
Proc Natl Acad Sci U S A. 1988 Nov; 85(21):7840-3.
[Proc Natl Acad Sci U S A. 1988]