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35 S‐labelled thiophosphorylated derivative of inositol trisphosphate
Author(s) -
Folk P.,
Kmoníčková E.,
Krpejšová L.,
Strunecká A.
Publication year - 1988
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.2580250713
Subject(s) - inositol , chemistry , thiophosphate , inositol phosphate , dephosphorylation , second messenger system , phosphomonoesterase , hydrolysis , sugar phosphates , inositol trisphosphate , phosphatase , inositol trisphosphate receptor , biochemistry , stereochemistry , phosphate , enzyme , receptor , organic chemistry
We have prepared the [ 35 S] thiophosphate labelled inositol trisphosphate and [ 32 P]phosphate labelled inositol trisphosphate (IP 3 ) from human erythrocytes. These compounds were used as substrates for the inositol trisphosphate 5‐phosphomonoesterase assay in human erythrocyte membranes. During 60 min incubation with the enzyme, the 35 S‐labelled IP 3 was not hydrolyzed, meanwhile the 32 P‐labelled IP 3 was broken down to 19.8 ± 2.4 %. This suggests that due to the presence of thiophosphate in the molecule the 35 S‐labelled IP 3 cannot serve as substrate for inositol trisphosphate 5‐phosphomonoesterase. The [ 35 S] thiophosphorylated derivative thus represents a nonhydrolyzable analogue of IP 3 and could be used in the study of its second messenger role.