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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1986-3-14
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
134
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37-43
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:3080989-Animals,
pubmed-meshheading:3080989-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3080989-Glucan 1,4-alpha-Glucosidase,
pubmed-meshheading:3080989-Glucosidases,
pubmed-meshheading:3080989-Intestines,
pubmed-meshheading:3080989-Molecular Weight,
pubmed-meshheading:3080989-Multienzyme Complexes,
pubmed-meshheading:3080989-Protein Biosynthesis,
pubmed-meshheading:3080989-Rats,
pubmed-meshheading:3080989-Sucrase-Isomaltase Complex
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pubmed:year |
1986
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pubmed:articleTitle |
In vitro translation of intestinal sucrase-isomaltase and glucoamylase.
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pubmed:publicationType |
Journal Article
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