Purification and partial sequencing of bovine liver alkaline phosphatase

Jia Cheng Hua, Enrico Garattini, Yu Ching E Pan, Jeffrey D. Hulmes, May Chang, Larry Brink, Sidney Udenfriend

Research output: Contribution to journalArticlepeer-review


Bovine liver alkaline phosphatase has been purified to homogeneity by procedures that include reverse-phase HPLC. The pure enzyme has an apparent Mr of 160,000 and is composed of what appears to be two identical monomers of Mr 82,000. About 80% of the material yielded the amino-terminal sequence Leu-ValProGluLysGlu LysAspPro?Tyr?ArgAspGlnAlaGln. The minor component was extended at the amino terminus by two residues that have not yet been identified, i.e., ?? LeuValProGluLysGluLysAspPro?Tyr?Arg AspGlnAlaGln.

Original languageEnglish
Pages (from-to)380-385
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - 1985

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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