Properties of nucleosides diphosphatases in purified membrane fractions from maize coleoptiles, 1: study of latency
M'Voula Tsieri, M.
Properties of nucleosides diphosphatases in purified membrane fractions from maize coleoptiles, 1: study of latency - 1981 - Printed
18 ref.; Summary (En)
Evidence is given for the presence of nucleoside diphosphatase (NDPase) activities in two membrane fractions from maize coleoptiles, one enriched in endoplasmic reticulum (ER) and the other in plasma membranes (PM). The NDPase activity associated with the ER-rich fraction appears only after treatment of membranes with detergent. Enzyme inactivation experiments using trypsin were performed on intact and Triton X-100-treated vesicles. They suggest that in the endoplasmic reticulum-rich fraction, most of enzymatic sites have a lumenal location and that in plasma membrane vesicles, only 40-50 per cent of enzymatic sites are not freely accessible to nucleosides
English
Maize
Zea mays
81-663982
Properties of nucleosides diphosphatases in purified membrane fractions from maize coleoptiles, 1: study of latency - 1981 - Printed
18 ref.; Summary (En)
Evidence is given for the presence of nucleoside diphosphatase (NDPase) activities in two membrane fractions from maize coleoptiles, one enriched in endoplasmic reticulum (ER) and the other in plasma membranes (PM). The NDPase activity associated with the ER-rich fraction appears only after treatment of membranes with detergent. Enzyme inactivation experiments using trypsin were performed on intact and Triton X-100-treated vesicles. They suggest that in the endoplasmic reticulum-rich fraction, most of enzymatic sites have a lumenal location and that in plasma membrane vesicles, only 40-50 per cent of enzymatic sites are not freely accessible to nucleosides
English
Maize
Zea mays
81-663982