脱落酸对离体水稻叶片衰老及其纤维素酶活力的影响

在脱落酸(ABA)促进离体水稻叶片衰老过程中,叶绿素含量日渐下降,纤维素酶活力日益升高。ABA 作用的滞后期为48小时。衰老叶片的胞壁附有大量的纤维素酶。酶从胞内分泌到胞壁,是与质膜结构受到损害,使透性增大有关。6-苄氨基嘌呤(6-BA)与 ABA 的相互作用对纤维素酶活力的影响表明,ABA 引起的水稻叶片衰老可分为两个阶段:在0到1天,6-BA近乎完全逆转 ABA 的效应,第二天有所减弱,这是可逆期;从第三天起,6-BA 对 ABA 几无拮抗作用,为不可逆期开始。     

蓝光延缓绿豆离体叶片衰老的研究

当绿豆幼苗在自然条件下生长到12d龄时,剪下第一对叶片,漂浮在水面,以蓝光荧光灯照射叶片,用白光和黑暗为对照。蓝光处理可延缓叶片叶绿素和蛋白质含量的降低,促进气孔的开放,维持SOD活性在较高的水平,从而延缓了质膜相对透性的增大。因此,我们认为,蓝光可以延缓绿豆幼苗离体叶片的衰老。     

STUDIES ON PROTEIN SYNTHESIS IN TOMATO COTYLEDONS AND LEAVES. I. PROTEIN SYNTHESIS AND TURNOVER IN INTACT COTYLEDONS AND LEAVES

1. Details of aseptic culture of virus-free tomato seedlings usedin comparative in vivo and in vitro studies on protein synthesisare described.
2. Developmental changes in the levels of DNA,RNA, protein andchlorophyll content of seedling cotyledonsand leaves were recorded,and are related to protein synthesis.
3. Incorporation of isotopically labeled carbon into proteinwasfollowed both by photosynthetic uptake of ¹⁴CO₂ and by theuptakeof ¹⁴C-amino acids through the roots.
4. A marked stimulationby light of ¹⁴C uptake was observed, andthe higher rate of¹⁴C incorporation from ¹⁴CO₂ than from ¹⁴C-aminoacids intothe protein fraction is discussed in relation tothe pathwaysof protein synthesis in tomato leaves, and alsowith regardto protein turnover.

¹Present address: Dept. of Horticultural Science, Universityof Wisconsin, U.S.A.     

Studies on Foliar Penetration: IX. PATTERNS OF PENETRATION OF 2,4-DICHLOROPHENOXYACETIC ACID INTO THE LEAVES OF DIFFERENT SPECIES

The comparative patterns of penetration of 2,4-dichlorophenoxyaceticacid (2,4-D) into the leaves of Phaseolus vulgaris, Zea mays,Pisum sativum, Beta wlgaris, Helianthus annuus and Gossypiumhirsuium have been examined. Save for Zea and Gossypium where there is little change withthe stage of leaf development the rates of penetration intoboth surfaces decrease as the leaf matures. The relative ratesare dependent on the species and the age of the leaf but thereare differences between the surfaces. In Phaseolus the characteristicsof primary leaves differ from those of trifoliate leaves sinceonly in immature trifoliate leaves is penetration into the adaxialsurface greater. In darkness the rates of penetration over 24 h remain constantor fall but slightly for all species. Light consistently promotespenetration but with Beta there is a lag before entry is acceleratedinto the abaxial surface as has previously been reported foryoung primary leaves of Phaseolus. For the remaining speciesthe courses of penetration in both light and darkness into bothsurfaces follow similar patterns. As the light intensity isincreased entry is enhanced but the limit of response variesbetween species, between surfaces within species, and in trifoliateleaves of Phaseolus with age. For the six species the order of the relative rates of entryis closely similar whether comparisons are made in light ordarkness or between abaxial and adaxial surfaces: viz. Zea >Helianthus > Phaseolus (primary) > Phaseolus (trifoliate)> Pisum = Beta = Gossypium. The observed specific differencesare discussed in relation to variations in leaf structure, theproperties and thickness of the cuticle and the physiologicaland metabolic processes which influence transport within theepidermal tissues after it has passed through the cuticle bydiffusion.     

STUDIES ON PROTEIN SYNTHESIS IN TOMATO COTYLEDONS AND LEAVES. II. INTERMEDIATE STAGES OF PROTEIN SYNTHESIS

1. The activities of RNase, ATPase and proteolytic enzymes inextractsof tomato leaves have been investigated with regardto detrimentaleffects on protein synthesis. The use of coppersulphate asan inhibitor of RNase is described.
2. The effectof microbial contamination on amino acid uptake hasbeen studiedin relationship with cell-free systems, and thehigh activitynoted underlines the necessity for aseptic procedures.
3. Methodsfor the preparation of cell-free systems capable ofamino acidactivation and incorporation into protein in an asepticenvironmentare discussed.

¹Present address: Dept. of Horticultural Science, Universityof Wisconsin, Madison, Wisconsin, U.S.A.