Human liver alkaline phosphatase, purification and partial sequencing: Homology with the placental isozyme

Enrico Garattini, Jia Cheng Hua, Yu Ching E Pan, Sidney Udenfriend

Research output: Contribution to journalArticle

Abstract

Human liver alkaline phosphatase (AP) has been purified to homogeneity. The enzyme has a molecular weight of 150,000 in its native state and consists of two identical subunits of Mr 75,000. After treatment with endoglycosidase F the molecular weight is reduced to 50,000 indicating a high degree of glycosylation. The amino-terminal sequence up to 22 residues was found to be LeuValProGluLysGluLysAspProLys Tyr(Ala)ArgAspGlnAlaGln?ThrLeuLysTyr. The amino-terminal portions of human and bovine liver AP are identical. The amino termini of the human liver and human placental AP isozymes have appreciable homology. Conformationally the amino termini are very similar.

Original languageEnglish
Pages (from-to)331-337
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume245
Issue number2
DOIs
Publication statusPublished - 1986

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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