Amino Acid Sequence of Escherichia coli Alkaline Phosphatase. Amino- and Carboxyl-Terminal Sequences and Variations between Two Isozymes

Philip M. Kelley, Peter A. Neumann, Karen Shriefer, Fiorella Cancedda, Milton J. Schlesinger, Ralph A. Bradshaw

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

The amino- and carboxyl-terminal fragments of E. coli alkaline phosphatase, produced by cyanogen bromide cleavage, have been isolated. The carboxyl-terminal fragment, CB-VI, contains seven amino acid residues in the sequence Lys-Ala-Ala-Leu-Gly-Leu-Lys. The absence of homo-serine and the coincidence of carboxyl-terminal lysine in native alkaline phosphatase suggest the carboxyl-terminal assignment. The amino-terminal fragment, CB-VII, contains five and four residues when isolated from isozymes 1 and 3, respectively. CB-VII from isozyme 1 possesses the sequence Arg-Thr-Pro-Glu-HSe. The corresponding peptide from isozyme 3 is devoid of the argininyl residue. Amino-terminal analyses of native alkaline phosphatase suggest the amino-terminal alignment of CB-VII. Analyses for carbohydrate indicate both isozymes are devoid of those sugars commonly found in glycoproteins.

Original languageEnglish (US)
Pages (from-to)3499-3503
Number of pages5
JournalBiochemistry
Volume12
Issue number18
DOIs
StatePublished - Aug 1 1973

ASJC Scopus subject areas

  • Biochemistry

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