Abstract:
:In this investigation we report the presence of two forms of inositol (1,4,5)P3/(1,3,4,5)P4-polyphosphate 5-phosphatase activity (types I and II) which were observed in soluble extracts of skeletal muscle after fractionation by DEAE-Sephacel chromatography. Hydrolysis of D-myo-inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) and D-myo-inositol 1,3,4,5-tetrakisphosphate by both phosphatases was 5-phosphate-specific, Mg2+ ion-dependent and inhibited by D-2,3-bisphosphoglycerate. Soluble type I 5-phosphatase activity was purified 27,300-fold to a specific activity of 2.54 mumol of Ins(1,4,5)P3 hydrolyzed/min/mg protein after a combination of DEAE-Sephacel, Blue Sepharose, heparin-agarose and structural analogue affinity chromatography. Purified type I 5-phosphatase had an apparent mean Km of 8.9 and 1.1 microM and Vmax of 3.55 and 0.13 mumol of substrate hydrolyzed/min/mg protein for Ins(1,4,5)P3 and Ins(1,3,4,5)P4, respectively. Investigations on soluble type II 5-phosphatase after DEAE-Sephacel chromatography indicated an apparent Km of 71.4 microM Ins(1,4,5)P3 and an apparent molecular mass of 81 kDa. Soluble type I phosphatase has an apparent molecular mass of 48 kDa and an isoelectric point of 5.8. Soluble type I 5-phosphatase has kinetic constants which suggest a role in the regulation of inositol polyphosphates at physiological concentrations. These results support a role for Ins(1,4,5)P3 in the regulation of Ca2+ homeostasis in skeletal muscle.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Hansbro PM,Foster PS,Hogan SP,Ozaki S,Denborough MAdoi
10.1006/abbi.1994.1207subject
Has Abstractpub_date
1994-05-15 00:00:00pages
47-54issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(84)71207-0journal_volume
311pub_type
杂志文章abstract::The cytosol fraction of an extract of Xenopus laevis ovaries contains a protein inhibitor that can specifically block the activation of calmodulin-sensitive cyclic nucleotide phosphodiesterase (PDE I) found in that tissue. This inhibitor was purified by DEAE-cellulose chromatography, gel filtration on Sephacryl S-200,...
journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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