Cloning and sequencing of human intestinal alkaline phosphatase cDNA

J. Berger, E. Garattini, J. C. Hua, S. Udenfriend

Research output: Contribution to journalArticle

114 Citations (Scopus)

Abstract

Partial protein sequence data obtained on intestinal alkaline phosphatase indicated a high degree of homology with the reported sequence of the placental isoenzyme. Accordingly, placental alkaline phosphatase cDNA was cloned and used as a probe to clone intestinal alkaline phosphatase cDNA. The latter is somewhat larger (3.1 kilobases) than the cDNA for the placental isozyme (2.8 kilobases). Although the 3' untranslated regions are quite different, there is almost 90% homology in the translated regions of the two isozymes. There are, however, significant differences at their amino and carboxyl termini and a substitution of an alanine in intestinal alkaline phosphatase for a glycine in the active site of the placental isozyme.

Original languageEnglish
Pages (from-to)695-698
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number3
Publication statusPublished - 1987

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Isoenzymes
Organism Cloning
Complementary DNA
Alkaline Phosphatase
3' Untranslated Regions
Alanine
Glycine
Catalytic Domain
Clone Cells
human ALPI protein
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Cloning and sequencing of human intestinal alkaline phosphatase cDNA. / Berger, J.; Garattini, E.; Hua, J. C.; Udenfriend, S.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 84, No. 3, 1987, p. 695-698.

Research output: Contribution to journalArticle

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