Effect of shade treatment on biosynthesis of catechins in tea plants

When tea plants were shaded with black lawn cloth for severaldays in the field, the accumulations of (—)-epicatechin,(—)-epicatechin-3-gallate, (—)-epigallocatechinand (—)-epigallocatechin-3-gallate decreased in newlydeveloping tea shoots. Radioactive tracer studies showed thatthe conversions of glucose-U-¹⁴C, shikimic acid-G-¹⁴C and phenylalanine-U-¹⁴Cinto (—)-epicatechin and (—)-epigallocatechin moietieswere depressed by the shade treatment for tea plants but theincorporation of trans-cinnamic acid-3-¹⁴C was not affected.The treatment was found to have no significant effect on theactivities of phospho-2-keto-3-deoxy-heptonate. aldolase (EC.4.1.2.15 [EC] ), 3-dehydroquinate synthase (EC. 4.6.1.3 [EC] ), 3-dehydroquinatedehydratase (EC. 4.2.1.10 [EC] ), shikimate dehydrogenase (EC. 1.1.1.25 [EC] )and trans-cinnamate 4-monooxygenase (EC. 1.14.13.11 [EC] ) in theshoots, whereas the activity of phenylalanine ammonia-lyase(EC. 4.3.1.5 [EC] ) clearly decreased. (Received March 17, 1980; )     

Lipid Peroxidation by the [Peroxidase/H2O2/Phenolic] System

Linoleic acid was oxygenated by horseradish peroxidase (EC 1.11.1.7 [EC] )in the presence of phenolics. The phenolics effective for thissystem had substituents at the P-position. The peroxidase-dependentlipid peroxidation produced reaction products similar to thoseproduced by lipoxygenase (EC 1.13.1.13 [EC] ) under the same conditions.Positional isomers of the reaction products were identifiedas 13-hydroperoxy-9, lloctadecadienoic acid and 9-hydroperoxy-10,12-octadecadienoicacid. (Received November 15, 1986; Accepted March 19, 1987)     

The effect of n-propyl gallate on the formation of ethylene during protoplast isolation in sugarbeet (Beta vulgaris L.)

The formation of ethylene during isolation of mesophyll protoplastsfrom leaves of in vitro cultured sugarbeet (Beta vulgaris L.)seedlings was monitored. The addition of the lipoxygenase (EC1.13.11.12 [EC] ) inhibitor n-propyl gallate to the isolation mediumsignificantly reduced the amount and rate of ethylene production.The relevance of cell physiology on protoplast regenerationis discussed. Key words: Beta vulgaris L., protoplasts, ethylene, lipoxygenase inhibitor, regeneration     

Collapse of Peroxide-Scavenging Systems in Apple Flower-Buds Associated with Freezing Injury

Changes in the metabolic activities of peroxide-producing systemsand peroxide-scavenging systems after freezing and thawing inflower buds of the apple, Malus pumila Mill., were studied withspecial reference to freezing injury. In flower buds of the‘McIntosh’ apple that were frozen below lethal temperatures,the activity of NADH-Cyt c reductase (EC 1.6.99.3 [EC] ), one of theenzymes in the electron-transport chains that are related tothe peroxide-producing systems, decreased slightly, while thatof Cyt c oxidase (EC 1.9.3.1 [EC] ) hardly changed. By contrast, theactivities of glucose-6-phosphate dehydrogenase (EC 1.1.1.49 [EC] ),dehydroascorbate reductase (EC 1.8.5.1 [EC] ) and ascorbate peroxidase(EC 1.11.1.11 [EC] ), which are involved in the peroxide-scavengingsystems, decreased to very low levels. The activity of glyceraldehyde-3-phosphatedehydrogenase (EC 1.2.1.12 [EC] ) also decreased markedly. However,little change was observed in the activities of hexokinase (EC2.7.1.1 [EC] ), glucosephosphate isomerase (EC 5.3.1.9 [EC] ), glutathionereductase (EC 1.6.4.2 [EC] ) and glutathione peroxidase (EC 1.11.1.9 [EC] ).Examination of substrates involved in the peroxide-scavengingsystems revealed that the levels of glucose-6-phosphate andfructoses-phosphate decreased to approximately 10^–4 to10^–5 M and 10^–5 M, respectively, and the levelsof GSH decreased to about 10^–5 M or became barely detectable.A decrease in the levels of GSSG also occurred while levelsof ascorbate rose slightly. Similar results were observed withflower buds from ‘Starking Delicious’ and ‘Jonathan’apple trees. These results suggest that the freezing injury to apple flower-budsis closely related to the collapse of the peroxide-scavengingsystems that are coupled with the pentose phosphate cycle. Theresults also suggest that the dysfunction of these peroxide-scavengingsystems is caused by H₂O₂, which may be produced during freezingand thawing. (Received March 14, 1992; Accepted June 5, 1992)     

Some Biochemical Characteristics of Guard Cell and Mesophyll Cell Protoplasts from Commelina communis L.

Guard cell and mesophyll cell protoplasts of Commelina communisL., were isolated and used to investigate their various biochemicalcharacteristics. Contamination of the samples by other celltypes was very low and viability of the protoplasts, assessedby the use of neutral red, Evans blue and fluorescein diacetate,was high (89–98%). Mesophyll cell protoplasts containedmore chlorophyll (x 47), more soluble protein (x 10), more totalN (x 36) and more DNA (x 9) than guard cell protoplasts. Theabsorption spectra of protoplast extracts were similar for bothcell types except that below 400 nm there was a large increasein absorption by the guard cell protoplast extract. In guardcell protoplast extracts, high levels of activity of phosphoenolpyruvatecarboxylase (E.C. 4.1.1.31 [EC] ), NAD malate dehydrogenase (E.C.1.1,1.37), NADP malic enzyme (E.C. 1.1.1.40 [EC] ) and carbonic anhydrase(E.C. 4.2.1.1 [EC] ) were detected while only low levels of pyruvate-orthophosphatedikinase (E.C. 2.7.9.1 [EC] ) activity were detected. Glycollate oxidase(E.C. 1.1.3.1 [EC] ), ribulose-l,5-bisphosphate carboxylase (E.C 4.1.1.39 [EC] ),NADP malate dehydrogenase (E.C. 1.1.1.82 [EC] ) and NAD malic enzyme(E.C. 1.1.1.39 [EC] ) were not detected in guard cell protoplast extracts.High levels of ribulose-1, 5-bisphosphate carboxylase, glycollateoxidase, NAD malate dehydrogenase and carbonic anhydrase weredetected in mesophyll cell protoplast extracts which is typicalof C₃ plants. A pathway of carbon flow during stomatal openingand closing is proposed. Key words: Carbon metabolism, Commelina communis, guard cell protoplasts, mesophyll cell protoplasts, stomata     

Senescence- and drought-related changes in peroxidase and superoxide dismutase isoforms in leaves of Ramonda serbica

Ramonda sp. (Gesneriaceae) is an endemic and relic plant ina very small group of poikilohydric angiosperms that are ableto survive in an almost completely dehydrated state. Senescence-and drought-related changes in the activity of peroxidase (POD;EC 1.11.1.7 [EC] ), ascorbate peroxidase (EC 1.11.1.11 [EC] ), and superoxidedismutase (SOD; EC 1.15.1.1 [EC] ) were determined in leaves of differentage and relative water content. The results indicate that differentPOD isoforms were stimulated during senescence and dehydration.Two of the soluble POD isoforms were anionic with pI 4.5, andtwo were cationic with pI 9.3 and 9.0. The activity of ascorbateperoxidase remained unchanged either by drought or senescence.For the first time, SOD isoforms have now been determined inthis resurrection plant. Several SOD isoforms, all of the Mntype, were found to be anionic with pI 4 and a few others hadpI from 5 to 6, while one band of FeSOD with a lower molecularweight was neutral. Rehydration brought about a remarkable decreaseover the first hour in the activity of all the antioxidant enzymesexamined but activity recovered 1 d after rehydration. The resultsconfirmed that dehydration and senescence caused disturbancein the redox homeostasis of Ramonda leaves, while inducing differentPOD isoforms. A physiological role of peroxidase reaction withhydroxycinnamic acids in conservation and protection of cellularconstituents of desiccated Ramonda leaves is suggested. Key words: Desiccation, peroxidase, Ramonda, senescence, superoxide dismutase     

Scavenging of Hydrogen Peroxide in the Endosperm of Ricinus communis by Ascorbate Peroxidase

The fat-storing endosperm of Ricinus communis L. was found tocontain an ascorbate peroxidase (EC 1.11.1.11 [EC] ), which is nearlyas active as catalase (EC 1.11.1.6 [EC] ) in degradation of hydrogenperoxide (H₂O₂) at its physiological concentrations. This ascorbateperoxidase probably functions together with monodehydroascorbatereductase (EC 1.6.5.4 [EC] ) or dehydroascorbate reductase (EC 1.8.5.1 [EC] )and glutathione reductase (EC 1.6.4.2 [EC] ) to remove the H₂O₂ producedduring the transformation of fat to carbohydrate in the glyoxysomes.The activities of these enzymes as well as the content of ascorbateand glutathione increase parallel to the activities of glyoxysomalmarker enzymes during the course of germination. Inhibitionof catalase by aminotriazole results in increases of the ascorbateperoxidase activity and of the glutathione content. All fourenzymes are predominantly localized in the cytosol of the Ricinusendosperm with low activities found in the plastids and themitochondria. The results suggest, that the ascorbate-dependentH₂O₂ scavenging pathway, which has been shown to be responsiblefor the reduction of photosynthetically derived H₂O₂ in thechloroplasts, operates also in the Ricinus endosperm. (Received June 5, 1990; Accepted July 31, 1990)     

Change in Properties of Phosphoenolpyruvate Carboxylase in Kalanchoe daigremontiana with Leaf Age

The activity of phosphoenolpyruvate (PEP) carboxylase (EC 4.1.1.31 [EC] )increased with leaf age in Kalanchoe daigremontiana. Polyacrylamidegel electrophoresis showed 3 bands of PEP carboxylase activity,one predominant in young leaves, another predominant in olderleaves. PEP carboxylase activities in desalted extract differedaccording to pH, at acidic pH the enzyme activity of young leavesdecreased drastically, whereas that of older leaves remainednearly constant. (Received August 2, 1982; Accepted September 27, 1982)     

Glyoxylate Cycle Enzymes in Peroxisomes Isolated from Petals of Pumpkin (Cucurbita sp.) during Senescence

The activities of the two unique enzymes of the glyoxylate cycle,isocitrate lyase (EC 4.1.3.1 [EC] ) and malate synthase (EC 4.1.3.2 [EC] ),were undetectable in petals of pumpkin (Cucurbita sp. AmakuriNankin) until the end of blooming, but they appeared duringsenescence. The activity of catalase (EC 1.11.1.6 [EC] ) increased,glycolate oxidase (EC 1.1.3.1 [EC] ) activity did not change, whilehydroxypyruvate reductase (EC 1.1.1.81 [EC] ) activity peaked at fullblooming stage and declined thereafter. After fractionationof cellular organelles on a sucrose density gradient, we detectedisocitrate lyase and malate synthase activities in peroxisomalfractions only from petals at the senescing stage. Northernblot analysis revealed that malate synthase mRNA increased duringpetal senescence. Citrate synthase (EC 4.1.3.7 [EC] ) and malate dehydrogenase(EC 1.1.1.37 [EC] ) activities were also present, while aconitase(EC 4.2.1.3 [EC] ) was not detectable in peroxisomal fractions. Moreoverthe presence of 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35 [EC] )and urate oxidase (EC 1.7.3.3 [EC] ) in the peroxisomal fractionsfrom senescing petals indicates that peroxisomes could be involvedboth in the ß-oxidation pathway and in the purinecatabolism during petal senescence. (Received May 25, 1991; Accepted September 25, 1991)     

The Development of Activities of Some Enzymes Concerned with Glycollate Metabolism in Greening Bean Leaves

The activities of phosphoglycollate phosphatase (EC 3.1.3.18 [EC] ),glycollate oxidase (EC 1.1.3.1 [EC] .). catalase (EC 1.11.1.6 [EC] ), theperoxisomal NADH-glyoxylate reductase (EC 1.1.1.26 [EC] ) which isconsidered to function as a hydroxypyruvate reductase in theperoxisomes, and the chloro-plastic NADPH-dependent glyoxylatereductaae, have been measured in extracts prepared from 14-d-olddark-grown bean leaves during the course of their greening inresponse to exposure to continuous illumination. All of theenzymes were found in the dark-grown leaves and on a per-leafbasis the activities increased from 6- to 12-fold with the exceptionof a 2–3-fold increase of NADPH-dependent glyoxylate reductaseduring 96-h greening, while the activities either remained constantor declined during similar periods in darkness. Initial lagperiods were evident before the illumination-induced increasesin enzyme activities. As D-threo-chloramphenicol did not affectthe increase in activity of any of these enzymes it would appearthat the increases were in no way dependent on protein synthesisby 70S ribosomes, or on the development of photosynthetic activity.     

ATP Sulphurylase and O-Acetylserine Sulphydrylase in Isolated Mesophyll Protoplasts and Bundle Sheath Strands of S-deprived Maize Leaves

In Zea mays L. (cv. XL 72 A) leaves sulphur deficiency causedreduction of soluble protein and chlorophyll contents, whereasATP sulphurylase (EC 2.7.7.4 [EC] ) and O-acetylserine sulphydrylase(EC 4.2.95.9 [EC] ) activities increased with the increasing of S-deprivationtime. The two enzymes exhibited the maximum activity after 5d (ATP sulphurylase) and 3 d (O-acetylserine sulphydrylase)from the beginning of deprivation period. The activities weredifferently distributed between mesophyll protoplasts and bundlesheath strands. The results suggest that the activity of thetwo enzymes may be induced sequentially and differently regulatedin the two types of cells. Key words: ATP sulphurylase, Bundle sheath strands, Mesophyll protoplasts, O-acetylserine sulphydrylase, Sulphur deprivation, Zea     

Studies on the change of the respiratory system in roots in relation to the growth of plants II. Activity of iron-containing oxidases in roots of cereal crops with the aging of plants

Distribution of iron-containing oxidases in aging nodal rootsof rice and wheat was studied. Activities of cytochrome c oxidase(1.9.3.1 [EC] , cytochrome c : O₂ oxidoreductase), catalase (1.11.1.6 [EC] ,H₂O₂: H₂O₂ oxidoreductase) and peroxidase (1.11.1.7 [EC] , donor:H₂O₂ oxidoreductase) in wheat roots were comparatively higherthan were those in rice roots at corresponding stages. Cytochromec oxidase in roots remained active throughout the lives of therice and wheat crops. In rice roots, catalase seemed to playa distinct role around the panicle formation stage. Decay ofcatalase activity took place earlier than did that of peroxidaseand cytochrome c oxidase activities. In wheat roots similarenzyme activity changes were not observed. Data may suggestthat the high activity of iron containing oxidases at the panicleformation stage (I) may be chiefly due to catalase activityin rice roots. ¹Paper presented at the 14th Annual Meeting of the Society ofthe Science of Soil and Manure, Japan (1968). (Received November 21, 1968; )     

Antioxidant enzyme responses to chilling stress in differentially sensitive inbred maize lines

Antioxidant enzyme activities were determined at the first,third and fifth leaf stages of four inbred lines of maize (Zeamays L.) exhibiting differential sensitivity to chilling. Plantswere exposed to a photoperiod of 16:8 L:D for one of three treatments:(a) control (25C), (b) control treatment plus an exposure toa short-term chilling shock (11C 1 d prior to harvesting),and (c) long-term (11 C constant) chilling exposure. Catalase(CAT; EC 1.11.1.6 [EC] ), ascorbate peroxidase (ASPX; EC 1.11.1.11 [EC] ),superoxide dismutase (SOD; EC 1.15.1.1 [EC] ), glutathione reductase(GR; EC 1.6.4.2 [EC] ), and mono-dehydroascorbate reductase (MDHAR;EC 1.6.5.4 [EC] ) activities were assessed. Reducing and non-reducingsugars and starch concentrations were determined as generalmetabolic indicators of stress. Reduced activities of CAT, ASPX,and MDHAR may contribute to limiting chilling tolerance at theearly stages of development in maize. Changes in levels of sugarand starch indicated a more rapid disruption of carbohydrateutilization in comparison to photosynthetic rates in the chilling-sensitiveline under short-term chilling shocks and suggested a greaterdegree of acclimation in the tolerant lines over longer periodsof chilling. Key words: Antioxidant enzymes, differential chilling sensitivity, maize, soluble carbohydrates, Zea mays     

Kinetics of Phenylalanine Ammonia-Lyase and the Effect of L-{alpha}-aminooxy-{beta}-phenylpropionic Acid on Enzyme Activity and Radicle Growth in Germinating Lettuce Seeds

The effects of different concentrations of L--aminooxy-ß-phenyIpropionicacid (AOPP), an analog of L-phenylalanine, on the activity ofphenylalanine ammonia-lyase (PAL, EC 4.3.1.5 [EC] ) and the growthof radicles in 24 h old germinating lettuce (Lactuca salivaL.) seeds were investigated. AOPP causes a significant inhibitionof PAL activity in the seeds (85% inhibition at 10⁴ M). It alsocauses a stimulation of radicle growth at that concentration.The results show that the inhibition of PAL by AOPP may be dueto an irreversible binding of the inhibitor to the enzyme leadingto its inactivation. AOPP also inhibits ethylene biosynthesisin germinating lettuce seeds which could probably explain thestimulation of radicle growth in these seeds. The enzyme shows typical Michaelis-Menten kinetics. The K_m forL-phenylalanine is 4.2 x 10⁵ M. The enzyme does not show anytyrosine ammonia-lyase activity. Various substrate analogs suchas D-phenylalanine, p-fluorophenylalanine, ß-phenyllacticacid, tryptophan and the product of the enzyme reaction, trans-cinnamicacid, inhibit the enzyme competitively. A number of intermediatesand endproducts of the phenylpropanpid pathway, except chlorogenicacid, do not show any inhibition. ¹Scientific contribution number 1423 from the New HampshireAgricultural Experiment Station. (Received May 9, 1986; Accepted September 8, 1986)     

Anatomical and Biochemical Changes Associated with the Induction of Oilseed Rape (Brassica napus) Pod Dehiscence by Dasineura brassicae (Winn.)

Dehiscence of pods at an early stage of development is a characteristicof oilseed rape pods damaged by Dasineura brassicae (pod midge).Anatomical examination of pods exhibiting symptoms of infestationrevealed a loss of cohesion between intact cells of the dehiscencezone, a narrow tissue of thin-walled cells present between thevalve margins. Determination of hydrolytic enzyme activity inpericarp tissues of damaged siliquae showed localized enhancementof both polygalacturonase (EC 3.2.1.15 [EC] ) and cellulase (ß1,4 glucanase, EC 3.1.2.4 [EC] ) activity, positionally consistent withthese factors being responsible for the observed cell wall degradation.Mechanistic similarities of midge-induced and maturation-associatedpod dehiscence are discussed. Oilseed rape, Brassica napus L. cv., Bienvenu, pod shatter, pod midge, Dasineura brassicae (Winn.), cellulase, polygalacturonase     

Biosynthesis of Acyl Moieties of Capsaicin and its Analogues from Valine and Leucine in Capsicum Fruits

Biosynthetic pathways of acyl moieties of capsaicinoid in intactCapsicum fruits and spheroplasts prepared from placentas ofCapsicum fruits were examined using a radioisotopic technique.In intact Capsicum fruits, L-[U-¹⁴C] valine was incorporatedinto capsaicin and dihydrocapsaicin, the acyl constituents ofwhich are even-number branched chain fatty acids, while L-[U-¹⁴C]leucine was incorporated into nordihydrocapsaicin and homodihydrocapsaicin,which have odd-number branched chain facty acids as the acylmoieties. The intermediates of the odd- and even-number branchedchain fatty acids were identified with GLC/GPC after the spheroplastshad been incubated with L-[U-¹⁴C] valine or L-[U-¹⁴C] leucine.After incubation with L-[U-¹⁴C] valine, isobutyric acid and8-methyl nonanoic acid were detected, while isopentanoic acidand 9-methyl decanoic acid were found after incubation withL-[U-¹⁴C] leucine. The involvement of a-ketoisovalerate or a-ketoisocaproatein the biosynthesis of acyl moieties of capsaicinoid was alsodemonstrated in vitro using cell-free extracts of the placentasof Capsicum fruits. These findings suggest that the acyl moietiesof individual capsaicinoids in Capsicum fruits are synthesizedby pathways similar to those proposed for adipose tissue andbacteria. ¹Formation and Metabolism of Pungent Principle of Capsicum Fruits.Part IX. (Received September 2, 1980; Accepted November 17, 1980)     

The Regulation of the Starch-Malate Balances during Volume Changes of Guard Cell Protoplasts

The enzymatic activities of phosphoenolpyruvate carboxylase(EC 4.1.1.31 [EC] ), ‘malic enzyme’ (EC 1.1.1.40 [EC] ), phosphofmctokinase(EC 2.7.1.11 [EC] ) and fructosebisphosphatase (EC 3.1.3.11 [EC] ) weremeasured during the swelling and shrinking of isolated and purifiedguard cell protoplasts (Vicia faba) in darkness. The volumeincrease was accompanied by the activation of phosphofructokinaseand a short stimulation of phosphoenolpyruvate carboxylase,at the same time the ‘malic enzyme’ and fructosebisphosphatasewere inhibited. However, during the shrinkage of guard cellprotoplasts these two enzymes were activated in contrast tophosphoenolpyruvate carboxylase and phospho-fructokinase. Becauseof the dramatic increase of phosphoenolpyruvate carboxylaseactivity during the swelling, this enzyme was assumed to actas a trigger for the swelling phase.     

Development of Enzymes of the Glyoxylate Cycle during Senescence of Pumpkin Cotyledons

The presence and activities of isocitrate lyase (EC 4.1.3.1 [EC] )and malate synthase (EC 4.1.3.2 [EC] ) were studied during senescenceof pumpkin cotyledons (Cucurbita sp. Amakuri Nankin). Afterincubation of detached cotyledons in permanent darkness, theactivities appeared and increased up to the eighth day and thendeclined, while the activities of catalase (EC 1.11.1.6 [EC] ), glycolateox-idase (EC 1.1.3.1 [EC] ), and hydroxypyruvate reductase (EC 1.1.1.81 [EC] )decreased dramatically. After fractionation of cell organellesby sucrose density gradient, we detected isocitrate lyase andmalate synthase activities in peroxisomal fractions. The activityof the two key enzymes of the glyoxylate cycle also increasedduring senescence in vivo and we confirmed the presence of thetwo enzymes in the peroxisomal fractions after sucrose gradientcentrifugation. At every point examined, the level of malatesynthase was demonstrated by immunoblotting. It is concludedthat the development of isocitrate lyase and malate synthaseactivities represents the transition from leaf peroxisomes toglyoxysomes and that such a phenomenon is associated with senescence. (Received January 25, 1991; Accepted March 22, 1991)     

Structure and Function in the Grass Ligule: Mitochondria and Microbodies in the Membranous Ligule of Lolium temulentum L., an Ultrastructural and Cytochemical Study

The ultrastructure and distribution of the mitochondria andmicrobodies within the tissues of the ligule of mature leavesof Lolium temulentum L. are described. Staining of the mitochondriaand microbodies with diaminobenzidine (DAB) was observed. Mitochondrialstaining was totally inhibited by potassium cyanide and sodiumazide but not by aminotriazole, and did not occur in the presenceof added hydrogen peroxide; it was concluded that cytochromec oxidase (EC 1.9.1.3 [EC] ) was responsible. In the microbodies stainingwas reduced in the absence of added hydrogen peroxide and eliminatedin the presence of aminotriazole; it was concluded that catalase(EC 1.11.1.6 [EC] ) was responsible. Presence of succinic dehydrogenase(EC 1.3.99.1 [EC] ) activity was demonstrated in the mitochondriausing the copper-ferricyanide reaction; presence of sodium malonateand absence of sodium succinate greatly reduced mitochondrialdeposition of reaction product. The results are discussed inrelation to possible functions of these organelles in the ligule. Key words: Ligule, Lolium temulentum L., Enzyme ultracytochemistry     

Effects of Some Growth Regulators on Polyamine Biosynthetic Enzymes in Etiolated Pea Seedlings

This study was designed to examine possible links between polyaminebiosynthesis and effects of growth regulatory compounds. Anauxin (IAA), a cytokinin [benzyladenine; benzylaminopurine (BAP)],an ethylene source (ethephon) and abscisic acid (ABA) were individuallyapplied to terminal buds of excised etiolated or red light (R)-exposedpea epicotyls. Effects were noted on bud fresh weight and onthe two main enzymes of putrescine biosynthesis, arginine decarboxylase(ADC; EC 4.1.1.19 [EC] ) and ornithine decarboxylase (ODC; EC 4.1.1.17 [EC] ).As previously reported [Dai and Galston (1981) Plant Physiol.67: 266], both bud growth and ADC activity are increased byR light. In such buds, ADC is raised further by 1–10 µMBAP or ABA and inhibited by 1–10 µM IAA or ethylene(50 mg/liter or more of ethephon). In all cases, effects ofR-irradiation plus 1 mM growth regulators on ODC activity wasthe inverse of their effects on ADC, indicating independentcontrol of these pathways. These results do not support theview that putrescine biosynthetic activity is correlated withgrowth in etiolated pea seedlings. ¹Supported by a grant from NSF to A.W.G. ²Supported by a grant from the Turkish Government. Permanentaddress: Department of General Botany, University of Istanbul,S?leymaniye, Istanbul, Turkey. ³On sabbatical leave from the Department of Horticulture, HebrewUniversity of Jerusalem, Rehovot, Israel. (Received September 22, 1983; Accepted February 28, 1984)