In vitro translation of intestinal sucrase-isomaltase and glucoamylase

D. H. Alpers, D. Helms, S. Seetharam, V. L. May, A. W. Strauss

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


It is has been proposed that both sucrase-isomaltase and glucoamylase are initially synthesized as large single-chain precursors which are then processed to heterodimers. We have tested this hypothesis by in vitro translation of their mRNAs. The primary translation product of sucrase-isomaltase mRNA was a single polypeptide of Mr = 190,000. Similar experiments using antiserum against glucoamylase revealed a single polypeptide of Mr = 145,000. These results are consistent with the single chain precursor hypothesis for sucrase-isomaltase. However, the glucoamylase product (145 kDa) is too small to be processed to a heterodimer of Mr = 230,000. Moreover, the mature subunits (Mr = 135,000 and 125,000) probably are derived from the 145 kDa precursor by proteolytic trimming and must include and share most of the precursor protein.

Original languageEnglish
Pages (from-to)37-43
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Jan 14 1986


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