Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids

P. S. Henthorn, B. J. Knoll, M. Raducha, K. N. Rothblum, Clive A. Slaughter, M. Weiss, M. A. Lafferty, T. Fischer, H. Harris

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Abstract

Amino-terminal amino acid sequences (42 residues) were determined for the products of the three common alleles at the human placental alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] gene locus. The sequences differ at position 3, which is proline in types 1 and 2 but is leucine in type 3. cDNA libraries were constructed in phage λgt11 and used to isolate clones covering the coding regions of types 1 and 3 cDNAs. Comparison of the deduced amino acid sequences of the types 1 and 3 proteins showed 7 differences out of 513 amino acids, each due to a single base substitution. cDNA sequence comparisons showed three silent substitutions in the coding regions and three base differences in the greater than 1 kilobase pairs of 3' untranslated sequences.

Original languageEnglish (US)
Pages (from-to)5597-5601
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number15
DOIs
StatePublished - Dec 19 1986

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