English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

The 1282 bp cDNA of an isoenzyme of fructose-1,6- bisphosphatase was cloned from rat muscle. It shows 70% positional identity to the cDNA of rat liver fructose- 1,6-bisphosphatase and is clearly the product of a gene different from that coding for the liver enzyme. After cloning of the coding region of the rat muscle fructose-1,6-bisphosphatase cDNA in an expression vector, the recombinant enzyme could be detected in  E. coli  cell-free extracts by activity determination and Western blotting. Overexpressed fructose-1,6-bisphosphatase was found to be allosterically inhibited by AMP comparably to the enzyme isolated from rat muscle. Analysis of steady-state mRNA levels of various rat tissues with reverse-transcriptase polymerase chain reaction (RT-PCR) and Northern blotting revealed one or the two fructose-1,6-bisphosphatase isoenzyme mRNAs in most tissues tested with significant quantitative differences. Quantitative PCR using a homologous competitor showed that 1 μg of total RNA of rat muscle contains 1.7 × 10 6  molecules of rat muscle fructose-1,6-bisphosphatase mRNA. 3 × 10 4  copies of this message were found per μg total RNA of heart and kidney, respectively.

biological chemistry

Rat Muscle Fructose-1,6-Bisphosphatase: Cloning of the     cDNA, Expression of the Recombinant Enzyme, and Expression Analysis in     Different Tissues