Partial amino acid sequence of the preprotein form of the alpha subunit of human choriogonadotropin and identification of the site of subsequent proteolytic cleavage

S. Birken, J. Fetherston, J. Desmond, R. Canfield, I. Boime

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11 Scopus citations

Abstract

Messenger RNA isolated from first trimester placentae was translated using radiolabeled amino acids in both the wheat germ and the ascites cell-free systems. The choriogonadotropin α subunit product was purified by immunoprecipitation with a subunit specific antiserum. Its amino acid sequence was partially determined by automated Edman degradation analysis. An NH2-terminal extension of 24 amino acids was found and its partial sequence is: {A figure is presented}. The preprotein form of the subunit was cleaved by the addition of microsomal membranes resulting in a homogeneous NH2-terminal product. Hence, it is unlikely that this processing step accounts for the heterogeneity that has been observed previously in the structure of this region of the subunit.

Original languageEnglish
Pages (from-to)1247-1253
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume85
Issue number4
DOIs
StatePublished - Dec 29 1978

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