Partial amino acid sequence of human placental lactogen precursor and its mature hormone form produced by membrane-associated enzyme activity

Steven Birken, Donna L. Smith, Robert E. Canfield, Irving Boime

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

The precursor form of human placental lactogen, synthesized by a wheat germ extract cell-free system, has been partially sequenced and found to contain a high percentage of leucine residues within its first 20 amino acids. The partial NH2-terminal structure appears to be: {A figure is presented} The precursor form of hPL, produced by an ascites extract cell-free system, was cleaved by a membrane-associated enzyme into a form which exhibits the methionine and valine residues in NH2-terminal positions identical to those of native human placental lactogen.

Original languageEnglish
Pages (from-to)106-112
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume74
Issue number1
DOIs
StatePublished - Jan 10 1977

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