{"title":"Changes in carbohydrate and enzyme levels during the sink to source transition of leaves of Cucumis sativus L., a stachyose translocator","authors":"David M. Pharr, Harriet N. Sox","doi":"10.1016/0304-4211(84)90227-X","DOIUrl":"10.1016/0304-4211(84)90227-X","url":null,"abstract":"<div><p>The sink to source transition of expanding leaves of cucumber was studied by sampling leaves sequentially from the growing stem apex toward the base of the plant. Leaf fresh weight and photosynthetic rate increased in the progression to lower nodes. Sucrose and raffinose concentrations were higher in sink leaves than in source leaves. Galactinol and stachyose concentrations increased during leaf expansion. Both alkaline and acidic α-galactosidase activity declined during leaf expansion, whereas galactinol synthase activity increased abruptly in leaves beginning in the leaf at the fourth node below the apex. This increase in activity corresponded temporally to marked changes in the oligosaccharide composition of the leaves in favor of galactosyl-saccharides, particularly stachyose. Across all leaf positions, galactinol synthase correlated positively with galactosyl-oligosaccharide concentration (<em>r</em> = 0.90) and correlated negatively with sucrose concentration (<em>r</em> = −0.82). The ratio of stachyose to raffinose correlated positively with the ratio of galactinol synthase to α-galactosidase (<em>r</em> = 0.95). The results point to the importance of changes in enzyme levels per se as determinants of changes in soluble carbohydrate levels associated with acquisition of export capability during leaf expansion.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 3","pages":"Pages 187-193"},"PeriodicalIF":0.0,"publicationDate":"1984-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90227-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83679991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
J.P. Jacquot , M. Droux , M. Miginiac-Maslow , C. Joly , P. Gadal
{"title":"Frozen thylakoids: an improvement for reconstituted chloroplast enzyme light-activation systems","authors":"J.P. Jacquot , M. Droux , M. Miginiac-Maslow , C. Joly , P. Gadal","doi":"10.1016/0304-4211(84)90226-8","DOIUrl":"10.1016/0304-4211(84)90226-8","url":null,"abstract":"<div><p>This paper describes a new method for improving both the stability and reproducibility of chloroplast enzyme light-activation systems. Usually, the most labile components of these systems are the thylakoids, the preparation of which must be repeated daily. Freezing the thylakoids in small aliquots in liquid nitrogen and storing them at −90°C in a buffer containing 50% glycerol results in preparations whichare completely stable over an 18-month-period. Enzyme light-activation rates were essentially identical with either frozen or fresh thylakoids. Freezing, however, resulted in a slow decline of NADP-protoreduction rates and also in a gradual uncoupling of non-cyclic photophosphorylation.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 3","pages":"Pages 181-185"},"PeriodicalIF":0.0,"publicationDate":"1984-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90226-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85666123","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Two sites of phosphatidylcholine synthesis in the wheat aleurone cell","authors":"M.C. Wilkinson , D.L. Laidman , T. Galliard","doi":"10.1016/0304-4211(84)90228-1","DOIUrl":"10.1016/0304-4211(84)90228-1","url":null,"abstract":"<div><p>Sub-cellular fractions from radiolabelled wheat aleurone cells were isolated using two procedures. Using both procedures, [<em>methyl</em>-<sup>14</sup>C]choline, was actively incorporated into phosphatidylcholine in the aleurone grain and oleosome fractions, but [U-<sup>14</sup>C]glycerol was poorly incorporated. This was most apparent in quiescent seeds and seeds incubated for 14 h or less. It is proposed that phospholipid-synthesis in the aleurone grain and oleosome fractions takes place from pre-existing storage glycerolipids. In contrast, the microsome fraction incorporated both choline and glycerol. This was more predominant in seeds incubated for 24 h or more and presumably reflects turnover of phospholipids in the endomembrane system. The relevance of these results is discussed in relation to the biogenesis of endoplasmic reticulum in germinating wheat seeds.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 3","pages":"Pages 195-199"},"PeriodicalIF":0.0,"publicationDate":"1984-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90228-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86992363","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Growth hormones as a selection tool for somatic hybridization in Petunia","authors":"Rachel Ettinger-Paltin, Shamay Izhar, Dvora Swartzberg, Yona Tabib","doi":"10.1016/0304-4211(84)90234-7","DOIUrl":"10.1016/0304-4211(84)90234-7","url":null,"abstract":"<div><p>The growth hormones 6-benzylaminopurine (BAP), naphthaleneacetic acid (NAA) and 2,4-dichlorophenoxy-acetic acid (2,4-D) were used as a selection tool in some protoplast fusion experiments involving different inbred lines of <em>Petunia</em>. The efficiency of the selection scheme, the possibility of cross-feeding, and the reaction of the tissue to 2,4-D at different development stages are described. The selection scheme was proved highly efficient in experiments carried out by Izhar et al., Mol. Gen. Genet., 190 (1983) 468 and S. Izhar (unpublished), with only a negligible amount of cross-feeding between protoplasts of different lines. Lines sensitive to 2,4-D sprays require 2,4-D for protoplast division and tissue development to callus, while the lines resistant to 2,4-D sprays were not able to use 2,4-D for protoplast division and development.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 3","pages":"Pages 231-235"},"PeriodicalIF":0.0,"publicationDate":"1984-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90234-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76622011","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Methylation of rRNA genes in some higher plants","authors":"N.Steele Scoot , T.A. Kavanagh , Jeremy N. Timmis","doi":"10.1016/0304-4211(84)90231-1","DOIUrl":"10.1016/0304-4211(84)90231-1","url":null,"abstract":"<div><p>Cytosine residues were more heavily methylated in rDNA isolated from fruit nuclei of marrow, melon, cucumber and tap root nuclei of turnip, than in total DNA preparations. The rRNA genes showed varying degrees of heterogeneity for both length and methylation as assessed by digestion with restriction endonucleases. Marrow rDNA was not digested by the methylation sensitive restriction endonuclease HpaII and while none of the other rDNAs was extensively digested, cucumber rDNA showed a different pattern of heterogeneity following HpaII digestion to that shown following EcoRI digestion. Cloned (unmethylated) rDNA sequences were extensively digested by HpaII. The relatively high level of methylation of the rRNA genes may be related to the large number of these genes in higher plants.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 3","pages":"Pages 213-217"},"PeriodicalIF":0.0,"publicationDate":"1984-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90231-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77000768","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Irene Carlberg , Kristina Glimelius , Tage Eriksson
{"title":"Nuclear DNA-content during the initiation of callus formation from isolated protoplasts of Solanum tuberosum L","authors":"Irene Carlberg , Kristina Glimelius , Tage Eriksson","doi":"10.1016/0304-4211(84)90233-5","DOIUrl":"10.1016/0304-4211(84)90233-5","url":null,"abstract":"<div><p>Cytofluorimetric measurements of the DNA-content in the nuclei during the initiation of callus formation from isolated protoplasts of potato were performed using propidium iodide as fluorochrome. Reproducible measurements were obtained after digestion of the cell walls and after RNase treatment.</p><p>Nuclei with high DNA-content were found early in the culture and the frequency of these nuclei increased with time in culture. In addition to highly replicated nuclei, multinucleated cells were found, the frequency of which decreased during prolonged culturing.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 3","pages":"Pages 225-230"},"PeriodicalIF":0.0,"publicationDate":"1984-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90233-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74901560","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Plant regeneration by somatic embryogenesis from cultured young inflorescenses of Sorghum arundinaceum (Desv.) stapf. var. Sudanense (sudan grass)","authors":"C.J. Boyes, I.K. Vasil","doi":"10.1016/0304-4211(84)90189-5","DOIUrl":"10.1016/0304-4211(84)90189-5","url":null,"abstract":"<div><p>Somatic embryogenesis and subsequent plant regeneration was obtained from cultured young inflorescence segments of <em>Sorghum arundinaceum</em> var. <em>sudanense</em> (sudan grass). The inflorescences (10–50 mm in length) were cultured on Murashige and Skoog's medium supplemented with 0.01–5.0 mg/l 2,4-dichlorophenoxyacetic acid (2,4-D). A compact nodular callus and somatic embryos arose predominantly from the rachis. The best response was obtained from inflorescences 10 mm in length. Somatic embryos developed in 72% of the cultures on medium containing 1.0 mg/l 2,4-D. Regenerated plants were normal phenotypically and had 2<em>n</em>=20 chromosome number.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 2","pages":"Pages 153-157"},"PeriodicalIF":0.0,"publicationDate":"1984-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90189-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91494022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M. Laroche-Raynal, L. Aspart, M. Delseny, P. Penon
{"title":"Characterization of radish mRNA at three developmental stages","authors":"M. Laroche-Raynal, L. Aspart, M. Delseny, P. Penon","doi":"10.1016/0304-4211(84)90187-1","DOIUrl":"https://doi.org/10.1016/0304-4211(84)90187-1","url":null,"abstract":"","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"111 12 1","pages":"139-146"},"PeriodicalIF":0.0,"publicationDate":"1984-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76133259","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Brandon d. Moore, Maurice S.B. Ku, Gerald E. Edwards
{"title":"Isolation of leaf bundle sheath protoplasts from C4 dicot species and intracellular localization of selected enzymes","authors":"Brandon d. Moore, Maurice S.B. Ku, Gerald E. Edwards","doi":"10.1016/0304-4211(84)90186-X","DOIUrl":"https://doi.org/10.1016/0304-4211(84)90186-X","url":null,"abstract":"<div><p>A new source of cell wall digestive enzymes, Onozuka Cellulase RS (from <em>Trichoderma viride</em>), was evaluated for the effectiveness of leaf digestion and the release of bundle sheath protoplasts (BSP) in a variety of C<sub>4</sub> monocots and dicots. Several dicot species were identified from which BSP, as well as mesophyll protoplasts (MP), can readily be isolated by using the RS cellulase. Assays of marker enzymes, plus chlorophyll measurements, permitted analysis of protoplast yield and purity. BSP and MP have been purified (90–100%) from <em>Atriplex spongiosa</em> (NAD-malic enzyme (ME) subgroup) and from <em>Falveria trinervia</em> (NADP-ME subgroup), with final yields ranging from 6–24%.</p><p>Enzyme localization studies indicate that a substantial amount of NADP-malate dehydrogenase (DH) in <em>F. trinervia</em> occurs not only in the mesophyll chloroplasts, but also in the bundle sheath chloroplasts. Similar activities of an apparent NADP-utilizing malate dehydrogenase (but not activated by dithioerythritol, DTE) occurs in the mitochondria of bundle sheath cells of <em>A. spongiosa</em>. Aspects of the potential role of this enzyme in photosynthetic metabolism are further discussed.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":"35 2","pages":"Pages 127-138"},"PeriodicalIF":0.0,"publicationDate":"1984-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90186-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72271988","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}