Showing papers on "Polyamine binding published in 1989"
TL;DR: Putrescine, spermidine and spermine are natural components of carrot cell primary walls and their content depends on the age of the culture and is affected by different pH values and by the presence of Ca 2+ during wall extraction.
38 citations
TL;DR: Bulk isolation from protoplasts of Petunia and oat is attempted, finding that binding of labeled spermidine to a developmentally regulated 18 kilodalton protein in tobacco tissue cultures derived from thin surface layer explants is important.
Abstract: Previous work (A Apelbaum et al. [1988] Plant Physiol 88: 996-998) has demonstrated binding of labeled spermidine (Spd) to a developmentally regulated 18 kilodalton protein in tobacco tissue cultures derived from thin surface layer explants. To assess the general importance of such Spd-protein complexes, we attempted bulk isolation from protoplasts of Petunia and oat (Avena sativa). In Petunia, as in tobacco, fed radioactive Spd is bound to protein, but in oat, Spd is first converted to 1,3,-diaminopropane (DAP), probably by polyamine oxidase action. In oat, binding of DAP to protein depends on age of donor leaf and conditions of illumination and temperature, and the extraction of the DAP-protein complex depends upon buffer and pH. The yield of the DAP-protein complex was maximized by extraction of frozen-thawed protoplasts with a pH 8.8 carbonate buffer containing SDS. Its molecular size, based on Sephacryl column fractionation of ammonium sulfate precipitated material, exceeded 45 kilodaltons. Bound Spd or DAP can be released from their complexes by the action of Pronase, but not DNAse, RNAse, or strong salt solutions, indicating covalent attachment to protein.
36 citations
01 Jan 1989
TL;DR: This work attempted bulkisolation fromprotoplasts ofPetunia andoat and demonstrated binding oflabeled spermidine (Spd) toa developmentally regulated 18kilodalton protein intobacco tissue cultures derived fromthinsurface layer explants, indicating covalent attachment toprotein.
Abstract: Previous work(AApelbaum etal.[1988] Plant Physiol 88:996998)hasdemonstrated binding oflabeled spermidine (Spd) toa developmentally regulated 18kilodalton protein intobacco tissue cultures derived fromthinsurface layer explants. Toassessthe general importance ofsuchSpd-protein complexes, we attempted bulkisolation fromprotoplasts ofPetunia andoat(Avena sativa). InPetunia, asintobacco, fedradioactive Spdisboundto protein, butinoat,Spdisfirst converted to1,3,-diaminopropane (DAP), probably bypolyamine oxidase action. Inoat,binding of DAPtoprotein depends on ageofdonorleaf andconditions of illumination andtemperature, andtheextraction oftheDAPprotein complex depends uponbuffer andpH.Theyield ofthe DAP-protein complex was maximized byextraction offrozenthawedprotoplasts witha pH8.8carbonate buffer containing SDS.Itsmolecular size, basedonSephacryl columnfractionation ofammoniumsulfate precipitated material, exceeded 45kilodaltons.BoundSpdorDAPcanbereleased fromtheir complexes bytheaction ofPronase, butnotDNAse,RNAse, orstrong salt solutions, indicating covalent attachment toprotein.