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Literature DB >> 1847882

Demonstration of fructose 1,6-bisphosphatase in human term placenta.

Abstract

A proteolysed form of fructose 1,6-bisphosphatase (Fru-P2ase) has been detected and characterized in human term placenta. The extract was found to contain very low levels of activity with an alkaline pH optimum. Western blotting demonstrated a polypeptide of Mr 26,000, instead of the subunit of Mr 36,000 observed in native mammalian Fru-P2ases.

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Year: 1991 PMID： 1847882 DOI： 10.1007/bf02041255

Source DB: PubMed Journal: Experientia ISSN： 0014-4754

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References

23 in total

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Authors: K Nakashima; K Ogino
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Authors: W J Black; A Van Tol; J Fernando; B L Horecker
Journal: Arch Biochem Biophys Date: 1972-08 Impact factor: 4.013

Demonstration of fructose 1,6-bisphosphatase in human term placenta.

1. D-fructose-1,6-diphosphatase activity in rat placenta.

2. Modification of fructose bisphosphatase by a proteolytic enzyme from rat liver lysosomes.

3. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.

4. Regulation of rabbit liver fructose-1,6-diphosphatase. II. Modification by lysosomal cathepsin B1 from the same cell.

5. Isolation of ahighly active fructose diphosphatase from rabit muscle: its subunit structure and activation by monovalent cations.

6. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

7. Cathepsin M: a lysosomal proteinase with aldolase-inactivating activity.

Review 8. Regulation of fructose-bisphosphatase activity.

9. Glucose metabolism by human placental villi.

10. Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate.