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     

Differentiation of Photorespiratory Activity between Mesophyll and Bundle Sheath Cells of C4 Plants I. Glycine Oxidation by Mitochondria

Mitochondria were isolated from mesophyll protoplasts and bundlesheath protoplasts or strands which were obtained by enzymaticdigestion of six C₄ species: Zea mays, Sorghum bicolor, Panicummiliaceum, Panicum capillare, Panicum maximum and Chloris gayana,representative of three C₄ types. Photorespiratory glycine oxidationand related enzyme activities of mesophyll and bundle sheathmitochondria were compared. Mesophyll mitochondria showed good P/O ratios with malate andsuccinate as substrate but lacked the ability to oxidize glycine.On the other hand, mitochondria isolated from bundle sheathprotoplasts of P. miliaceum and bundle sheath strands of Z.mays possessed glycine oxidation activity similar to that ofmitochondria from C₃ plant leaves. The two enzymes involvedin glycine metabolism in mitochondria, serine hydroxymethyltransferaseand glycine decarboxylase, were also assayed in the mitochondriaof the two cell types. The activities of the two enzymes inbundle sheath mitochondria were in the range found in C₃ mitochondria.In contrast, the activities in mesophyll mitochondria were eithernot detectable or far lower than those in bundle sheath mitochondriaand ascribed to contaminating bundle sheath mitochondria. The present results indicate the deficiency of a complete glycineoxidation system in mesophyll mitochondria and also a differentiationbetween mesophyll and bundle sheath cells of C₄ plants withrespect to the photorespiratory activities of the mitochondria. (Received June 8, 1983; Accepted August 29, 1983)     

In vitro salt tolerance of cell wall enzymes from halophytes and glycophytes

The halophyte Suaeda maritima grows optimally in high concentrations(40–60% seawater) of salt. In these conditions the concentrationof salt in the apoplast of the leaves is at least 500 mM, aconcentration which severely inhibits the activity of cytoplasmicenzymes of both glycophytes and halophytes. The in vitro salttolerance of a number of cell wall enzymes was assayed in thepresence of a range of concentrations of NaCl. There was nosignificant inhibition of the activity of galactosidase, glucosidase,peroxidase or xyloglucan endo-transglycosylase extracted fromSuaeda maritima by in vitro concentrations of NaCl up to atleast 1 M. In vitro salt tolerance of cell wall enzymes wasnot restricted to the halophyte, similar enzymes from the non-halophilicrelative Kochia tricophylla, and from the glycophytes Vignaradiata and Cicer arietinum, were inhibited little, or not atall, by the same concentrations of salt. Pectin esterase wassomewhat less tolerant, but activity at 500 mM NaCl was stillgreater than at 0 mM NaCl in both Suaeda and Vigna. It is concludedthat these enzymes of the cell wall compartment are much moresalt-tolerant than cytoplasmic enzymes of higher plants. Theresults are discussed in relation to conditions thought to pertainin the apoplast. Key words: Apoplast, cell wall enzymes, halophyte, salt tolerance, Suaeda maritima     

Characteristics of the Photosynthetic Metabolism of Carbon in Deuterated Chlorella ellipsoidea C-27

The photosynthetic metabolism of carbon in fully deuteratedcells of Chlorella ellipsoidea C-27 (D-Chlorella), obtainedby culture in medium prepared with 100 mol% D₂O, was characterizedby examining the activities of several enzymes and the levelsof metabolic regulators in a comparison with those of ordinarycells (H-Chlorella). The cellular content of starch in D-Chlorellawas more than twice that in H-Chlorella, whereas those of sucroseand glucose were significantly lower in D-Chlorella. Deuterationof Chlorella caused marked alterations in the activities ofenzymes involved in starch metabolism. There was a significantdecrease in the activity of phosphorylase, a catabolic enzyme,and a significant increase in the activity of starch synthase,an anabolic enzyme. These alterations are probably responsiblefor the increase in the amount of starch in cells. By contrast,no marked changes were observed in the activities of enzymesand the levels of metabolic inhibitors that are involved inthe synthesis of sucrose. It seems likely, therefore, that thedecrease in the amount of sucrose in D-Chlorella was causedmainly by a deficiency in sources of carbon in the cytoplasm,as a consequence of an increase in levels of starch in chloroplasts. (Received May 13, 1992; Accepted December 1, 1992)     

Boron deficiency effects on peroxidase, hydroxyproline, and boron in cell walls and cytoplasm of Helianthus annuus L. hypocotyls

Boron-deficient sunflower hypocotyls have, on a fresh weightbasis, more cytoplasmic and cell wall peroxidase, more cytoplasmichydroxyproline but equal cell wall hydroxyproline, and slightlyless cell wall boron, than controls. Incubation of either Bdeficientor control cell wall suspensions with Sclerotium rolfsii culturenitrate released 80% of the peroxidase activity, but only 14to 30% of the hydroxyproline. This differential extraction suggeststhat the hydroxyproline-containing protein of cell walls isnot identical with peroxidase. Boron deficiency increased thesusceptibility of cell walls to degradation by fungal enzymes,as measured by release of peroxidase and hydroxyproline, butnot by reduction in dry weight. ¹Scientific article No. A1847, Contribution No. 4756 of theUniversity of Maryland Agricultural Experiment Station. Thisresearch represents part of a thesis for the M.S. degree, Universityof Maryland, by J.B.S., Jr. This paper is dedicated to ProfessorHugh G. Gauch on the occasion of his sixtieth birthday. (Received December 5, 1972; )     

Fungal Associations: III. The Role of Pectic Enzymes on the Synergistic Relation between Rhizoctonia solani Kuhn and Fusarium solani Snyder and Hansen, in the Rotting of Potato Tubers

The greatest activity of protopectinase obtained from the growthof Rhizoctonia solani and Fusarium solani on autoclaved potatoplugs occurred at pH 6.5, and greatest activity of the ‘lossof viscosity’ enzyme was found at 6–5 for Rhizoctonia,and between 6.5 and 8.3 for Fusarium. Protopectinase enzymeobtained from double infections of the Fusarium spp. with Rhizoctonia,or by mixing the enzymes of individual Fusarium spp. with Rhizoctoniaenzyme, were more active than the enzymes from single inoculations.Cylindrocarpon radicicola enzyme was more active when obtainedfrom a pure culture than from double infection. Similarly, mixingthis enzyme with the enzyme of Rhizoctonia reduced its activity.The evidence indicated that the protopectinase of Rhizoctoniawas similar to that of Cylindrocarpon and differed from thatof the Fusarium spp. Using paper partition chromatography, two bands from Rhizoctoniacrude enzyme had a stimulatory effect on Fusarium enzyme, whileonly one band from Fusarium enzyme stimulated Rhizoctonia enzyme. The purified enzyme of Rhizoctonia degraded pectin to galacturonicacid. Fusarium pure enzyme degraded pectin to an intermediatestage. A mixture of the two enzymes degraded pectin to galacturonicacid, without the intermediate stage formed by Fusarium alonebeing detected. The role played by pectic enzymes upon the synergistic relationof Rhizoctonia solani and Fusarium solani on rotting potatotubers is discussed.     

The Chloroplast and Leaf Developmental Mutant, pale cress, Exhibits Light-conditional Severity and Symptoms Characteristic of its ABA Deficiency

The PALE CRESS gene (PAC) is essential for proper chloroplastand leaf development in Arabidopsis thaliana. The ability ofpac mutants to accumulate significantly more chlorophyll whengrown in low light conditions than in high light conditionssuggests that carotenoid deficiency is at least partly responsiblefor premature cessation of chloroplast development. In additionto accumulation of low levels of chlorophyll and carotenoidpigments,pac mutants are abscisic acid (ABA) deficient and havecharacteristics which may be explained by this deficiency. Theseinclude reduced seed viability and, in enclosed growth conditions,increased leaf growth. Plants transformed with an antisensePAC construct often bear viviparous embryos which may be symptomaticof a deficiency in ABA. Since carotenoids are precursors ofABA, a role for PAC in carotenoid biosynthesis is further supported.The nuclear-encoded, chloroplast-localized PAC protein has beenimplicated in the maturation of plastid-encoded mRNAs. Thus,PAC may affect the abundance of one or more chloroplast proteinswhich function in the synthesis or stability of carotenoids.Using thePROLIFERA gene as a marker for cell division, it isshown that cell division profiles in the pac shoot apex aredisrupted. pac leaves are relatively normal in size and shapedespite the light intensity-induced variability of leaf celldefects. Copyright 2000 Annals of Botany Company Abscisic acid, carotenoid, chloroplast development, leaf development, organismal theory, PALE CRESS,PROLIFERA , vivipary     

Mechanisms of Oxidation of Inorganic Electron Donors in Autotrophic Bacteria

The enzymatic reactions involved in the oxidation of sulfide,sulfite, thiosulfate, ferrous ions, ammonia, and nitrite arereviewed for Chlorobium limicola f. thiosulfato philum, Thiobacillusnovellus, Thiobacillus ferrooxidans, Nitrosomonas europaea,and Nitrobacter winogradskyi. The properties of the purifiedredox enzymes and of proteins that participate in the oxidationof the inorganic compounds in these autotrophic bacteria aresummarized, and the mechanisms of the oxidation of the inorganiccompounds are discussed on the basis of the interactions betweenthe redox enzymes and carriers. (Received December 21, 1995; Accepted May 29, 1996)     

Cloning and characterization of a sialidase from the murine histocompatibility-2 complex: low levels of mRNA and a single amino acid mutation are responsible for reduced sialidase activity in mice carrying the Neula allele

The Neu1 locus, in the S region of the murine histocompatibility-2complex, regulates the sialic acid content of several liverlysosomal enzymes. Three alleles, Neu1^a, Neu1^b, and Neu1^c, havebeen described on the basis of differential sialylation of theenzyme liver acid phosphatase. The Neu1^a allele occurs in asmall number of mouse strains, e.g., SM/J and is associatedwith sialidase deficiency. We recently described G9, a sialidasegene in the human major histocompatibility complex (Milner etal. (1997) J. Biol. Chem., 272, 4549–4558), and we nowreport the characterization of the equivalent gene in mouse.The protein product of the murine G9 gene is 409 amino acidsin length and is 83% identical to its human orthologue. Expressionof the murine G9 protein in insect cells has confirmed thatit is a sialidase, with optimal activity at pH 5. To elucidatethe basis of sialidase deficiency in mouse strains carryingthe Neu1^a allele, we have sequenced the G9 coding regions frommice carrying the three Neu1 alleles and hence defined the aminoacid sequence characteristic of each allotype. Of particularinterest is a Leu-209 to Ile mutation that is unique to theNeu1^a allotype and is associated with reductions in sialidaseactivity of 68% and 88% compared to the Neu1^b and Neu1^c allotypes,respectively, when these three protein variants are expressedin insect cells. Additional factors, such as differential expression,may also influence the activities of the Nen1 allotypes in vivo.We have observed that the level of G9 mRNA is substantiallyreduced in mice carrying the Neu1^a allele compared to the Neu1^b(85–95% reduction) and Neu1^c (70% reduction) alleles. H2 complex MHC Neu1 sialidase     

Cytokinins and the Growth Responses of Seedlings of Betula pendula Roth. and Acer pseudoplatanus L. to Nitrogen and Phosphorus Deficiency

Deficiencies in the supply of nitrogen and phosphorus broughtabout the cessation of shoot extension and the formation ofterminal resting buds in seedlings of Acer pseudoplatanus maintainedunder long days, whereas seedlings of Betula pendula maintainedunder the same conditions continued extension growth of themain axis over a long period, although they showed symptomsof nitrogen deficiency, including a reduced chlorophyll content.The endogenous cytokinin levels of the base/nucleoside fractionin leaves of B. pendula were significantly lower in the nitrogen-deficientplants than in the controls only 3 d after transfer to deficientconditions. Similar, though less marked, changes were observedin response to phosphorus deficiency. Changes in the levelsof cytokinin activity in the nucleotide fraction in responseto nitrogen deficiency were much less marked. No significantchanges in cytokinin levels of the base/nucleoside or nucleotidefractions could be detected in leaf material from seedlingsof A. pseudoplatanus, even after a nitrogen or phosphorus deficiencytreatment of 4 weeks. Application of exogenous benzyladenineto seedlings of B. pendula subjected to nitrogen deficiencyresulted in a rapid regreening and to outgrowth of inhibitedlateral buds after only 2 d.     

Study of Biomphalaria Tenagophila Tenagophila, B. t. Guaibensis and B. Occidentalis by Polymerase Chain Reaction Amplification and Restriction Enzyme Digestion of the Ribosomal RNA Intergenic Spacer Regions

Biomphalaria tenagophila tenagophila, B. tenagophila guaibensisand B. occidentalis are indistinguishable on the basis of shellmorphology and the majority of organs of the genital system.Only B. t. tenagophila is susceptible to infection with Schistosomamansoni. The identification of this species is important forepidemiological studies of schistosomiasis. Snails from differentsites in Brazil, Argentine and Uruguay were studied using thePolymerase Chain Reaction (PCR) and Restriction Fragment LengthPolymorphism (RFLP) of the Ribosomal RNA Internal TranscribedSpacers (ITS) using seven enzymes. Profiles resulting from digestionwith AluI showed some invariant species-specific products allowingcorrect identification of B. t. tenagophila, B. occidentalisand B. t. guaibensis. Profiles obtained with other enzymes didnot permit species identification as extensive intraspecificpolymorphism or invariant RFLP profiles were observed. Restriction profiles obtainedwith all enzymes were used to calculate the percentage of bandsharing between all individual snails and these data were usedfor a cluster analysis. A closer relationship between B. occidentalisand B. t. guaibensis than B. t. tenagophila and the subspeciesB. t. guaibensis was observed. Based on previous morphologicaldata and these molecular data, we propose grouping B. t. tenagophila,B. occidentalis and B. t. guaibensis into a B. tenagophila complex. (Received 22 December 1997; accepted 26 May 1998)     

Chlorophyll Deficiency Caused by a Specific Blockage of the C5-Pathway in Seedlings of Virescent Mutant Rice

Temperature-sensitive mutants of rice, designated virescent(v₁, v₂ and v₃), develop chlorophyll-deficient leaves at a restrictivetemperature (20°C) but develop nearly normal green leavesat a permissive temperature (30°C). Analysis of the chlorophyllbiosynthetic pathway in the virescent mutants indicated thatthe chlorophyll deficiency at the restrictive temperature wasdue to specific blockage of the C₅-pathway. Northern analysissuggested that the chlorophyll deficiency in the virescent mutantswas caused by specific inhibition of the expression of chloroplasttRNA^Glu. (Received October 22, 1993; Accepted January 25, 1994)     

The response of tomato roots (Lycopersicon esculentum Mill.) to iron deficiency stress: alterations in the pattern of protein synthesis

Dicotyledon plants adapt to iron (Fe) deficiency through a seriesof reactions that increase the ability of the plant to assimilateFe and to increase the efficiency of Fe utilization. In an attemptto gain an insight into these adaptive processes, the specificchanges in protein synthesis associated with the onset of theFe deficiency response in tomato roots (Lycopersicon esculentumMill cv. Rutgers) have been investigated. Roots were grown underFe—sufficient and —deficient conditions, and thepattern of protein synthesis was analysed by in vitro translationof root mRNA and by in vivo labelling of root proteins. Polypeptideswere resolved by two—dimensional polyacrylamide gel elec—trophoresis.Seven polypeptides were identified by in vitro translation,whose synthesis was significantly increased during Fe deficiency.The increase was probably specific to Fe deficiency in thatthe polypep—tide synthesis was not increased during phosphatedeficiency stress, was less prominent following prolonged Fedeficiency and was decreased following re—supply of Feto the hydroponic medium. The pattern of in vitro translation of mRNA isolated from Fe—deficientroots was compared to the results obtainedin vivo followingradiolabelling of proteins. In these analyses, eight polypeptideswere identified, tentatively including the seven polypeptidespreviously identified by in vitro translation. All polypeptideswere characterized with regard to molecular mass and pl andtheir localization in the cell, whether being membrane boundor soluble. It is suggested that members of this group of polypeptidesare involved in the response of the root to Fe deficiency: althoughtheir functions remain to be identified. Key words: In vitro protein synthesis, iron, iron deficiency, root, 2-dimensional PAGE     

Extreme Phosphate Deficiency Decreases the In Vivo CO2/O2 Specificity Factor of Ribulose 1,5-Bisphosphate Carboxylase-Oxygenase in Intact Leaves of Sunflower

Sunflower plants were grown under controlled environmental conditionswith either 0 or 10 mol m^–3 phosphate (Pi). From steady-statemeasurements of gas exchange and chlorophyll fluorescence madeon intact leaves, the in vivo CO₂/O₂ specificity factor (invivo K_sp) of ribulose 1,5-Aisphosphate carboxylase-oxygenase(Rubisco) was determined following two methods based on modelsof C₃ photosynthesis by Brooks and Farquhar (1985) and Peterson(1989). The two methods gave in vivo K_sp values for controlsunflower leaves which were similar to published values forhigher plants. Extreme Pi deficiency decreased in vivo K_sp,in sunflower leaves compared to adequate Pi. This suggests thatPi deficiency affected photorespiration less than photosynthesis.The decrease in in vivo K_sp may be due to a real change in theenzyme kinetics favouring oxygenation more than carboxylationor due to an increase in the number of CO₂ molecules releasedper oxygenation; in which case the observed decrease in thein vivo K_sp determined on intact leaves will not agree numericallywith the true K_sp of Rubisco determined in vitro using purifiedenzyme from the same leaf. We discuss the implications of therelatively large photorespiration in Pi-deficient sunflowerleaves with respect to the increased dissipation of photosyntheticelectrons and photorespiratory recycling of Pi in thechloroplaststroma. Although our results on in vivo K_sp suggested a relativelylarger photorespiratory potential in Pi-deficient than controlsunflower leaves, photosynthesis was insensitive to O₂ in Pi-deficientleaves; the possible reasons for this phenomenon are discussed.Under extreme Pi deficiency, O₂ sensitivity of photosynthesisis not a reflection of the in vivo photorespiratory rates. Determinationof in vivo K_sp of Rubisco is a useful approach to study thephotorespiratory potential of intact leaves. Key words: Chlorophyll fluorescence, phosphate deficiency, photorespiration, photosynthesis, PSII quantum yield, Rubisco specificity factor     

Sucrose and Nitrogen Supplies Regulate Growth of Maize Kernels

The growth of maize (Zea mays L.) kernels depends on the availabilityof carbon (C) and nitrogen (N) assimilates supplied by the motherplant and the capacity of the kernel to use them. Our objectiveswere to study the effects of N and sucrose supply levels ongrowth and metabolism of maize kernels. Kernel explants of Pioneer34RO6 were culturedin vitro with varying combinations of N (5to 30 m M) and sucrose (117 to 467 m M). Maximum kernel growthwas obtained with 10 m M N and 292 m M sucrose in the medium,and a deficiency of one assimilate could not be overcome bya sufficiency of the other. Increasing the N supply led to increasesin the kernel sink capacity (number of cells and starch granulesin the endosperm), activity of certain enzymes (soluble andbound invertases, sucrose synthase, and aspartate aminotransaminase),starch, and the levels of N compounds (total-N, soluble protein,and free amino acids), and decreased the levels of C metabolites(sucrose and reducing sugars). Conversely, increasing the sucrosesupply increased the level of endosperm C metabolites, freeamino acids, and ADPG-PPase and alanine transaminase activities,but decreased the activity of soluble invertase and concentrationsof soluble protein and total-N. Thus, while C and N are interdependentand essential for accumulation of maximum kernel weight, theyappear to regulate growth by different means. Nitrogen supplyaids the establishment of kernel sink capacity, and promotesactivity of enzymes relating to sucrose and nitrogen uptake,while sucrose regulates the activities of invertase and ADPG-PPase.Copyright 1999 Annals of Botany Company Zea mays, maize,, invertase, ADPG-PPase, media composition, sucrose, nitrogen, C/N.     

Cell Wall Degrading Enzymes in Cuscuta reflexa and Its Hosts

Pectin degrading enzymes, hemicellulose degrading enzyme andcellulose degrading enzymes were studied in Cuscuta reflexaRoxb., its susceptible hosts, Brassica campestris L., Cocciniaindica W. & A. Datura innoxia Mill, Helianthus annuus L.,Holoptelea indica Planch, Lantana camara L., Medicago sativaL., Manihot utilissima Pohl, Petunia hybrida X Hort exvilm,Pisum sativum L., Phaseolus vulgaris L. and Solanum nigrum L.and non-susceptible plants Ipomoea batata Lam. and Solanum tuberosumL. Pectin esterase and polygalacturonase were present in higheramounts in Cuscuta parasitic on P. vulgaris and S. nigrum, whichneeded more time for haustorial establishment. Exo-l, 4-ß-D-glucosidaseactivity was found in Cuscuta but could not be detected in itshosts. Xylanase and cellulase activity of host plants increasedwhile cellobiase activity decreased as a result of infectionby the parasite. Higher pectin esterase, polygalacturonase,xylanase and exo-l, 4-ß-D-glucosidase activities inthe haustorial region of the parasite is likely to bring aboutthe lysis of the cell wall of the host plant and thus facilitatethe penetration of the parasite haustoria into the host sieveelement, which is necessary for the transport of nutrients betweenthe host and the parasite. Key words: Cell wall degrading enzymes, Cuscuta reflexa     

Regulation of phosphatase synthesis by orthophosphate in cultured tobacco cells

Phosphatase activity in cultured tobacco cells XD-6 increasedremarkably under phosphate-deficient culture conditions. Suchan increase did not occur in the activities of -amylase, ß-galactosidase,succinate dehydrogenase and catalase under the same cultureconditions. By replenishment with Pi, the increase in totalphosphatase activity was suppressed and the specific activitywas reduced to a low level. The suppression of increase in theactivity resulted form a repression of de novo synthesis ofthe enzyme. Added Pi also suppressed the release of phosphataseinto the culture medium. The effect of Pi was found to be greaterthan the effect on the increase in the intracellular activity. At least three phosphatases were extracted from XD-6 cells.One of the enzymes increased when the phosphatase synthesiswas increased by phosphate deficiency. ¹ Present address: Laboratory of Applied Microbiology, Facultyof Agriculture, Yamagata University, Tsuruoka, Yamagata 997,Japan. (Received May 18, 1977; )     

The Mechanisms of Apple Bud Morphogenesis: Analysis and a Model

Information in the literature suggests that the process of applebud morphogenesis is controlled by the level of growth substances,notably gibberellins in the bud, and by the availability ofgrowth substrate (S). The spur buds of apples must contain acertain minimum number of nodes (N_m) before flower primordiacan be formed, and the process of bud morphogenesis can be describedby a rate of node production with time, t by the equation It is postulated that the parameter k_G is a function of thebalance between the enzymes systems in the bud, the rate ofsynthesis of the enzymes associated with the development offloral bud parts (floral enzymes) being inversely related tothe level of gibberellins (G) in the bud. The parameter k_G isa function of the nutritional state of the bud; a is a rateparameter, and i is a conversion factor. Node production rateis asymptotic with increase in S, but switches from high tolow values as G varies about a critical concentration. The implicationsof the model, which appears to describe most observations, arediscussed, and some suggestions for testing it are put forward.     

Partial Separation of Roots as a Means of Reducing the Effect of Competition between Two Grass Species

Root competition between the perennial grass Oryzopsis holciformisand the annual Avena sterilis causes strong suppression of theformer. Its development much improved, however, when a smallportion of its root system was transferred into an attachedcontainer in which no roots of Avena sterilis were allowed togrow. The most striking increase in weight and nutrient uptakeoccurred when the auxiliary non-competing roots grew in a nutrientsolution. A lesser but unmistakable increase occurred when theseroots grew in an NPK-enriched soil. A competing O. holciformis contained little nitrogen but supplythrough the auxiliary roots caused an appreciable increase inpercentage of nitrogen. It seems that the auxiliary roots wereable to correct a competition-induced nitrogen deficiency (lessso for phosphorus deficiency) in spite of their comparativelyinsignificant quantity The implications of these findings regarding natural communitiesgrowing in heterogeneous rooting mediums are discussed.     

Differentiation of Photorespiratory Activity between Mesophyll and Bundle Sheath Cells of C4 Plants II. Peroxisomes of Panicum miliaceum L.

Peroxisomes were isolated by sucrose density gradient centrifugationfrom mesophyll and bundle sheath protoplasts of a C₄ plant,Panicum miliaceum L. The equilibrium density in the gradientwas 1.25 for bundle sheath peroxisomes and 1.23 for mesophyllperoxisomes, the former density being similar to that of peroxisomesof wheat mesophyll protoplasts. Photorespiratory and other microbody enzymes were assayed forthe peroxisomes of P. miliaceum to detect possible differentiationat an enzyme level. The specific activities of photorespiratoryenzymes, except for hydroxypyruvate reductase, in bundle sheathperoxisomes were 40–60% of those in wheat peroxisomes,when compared on a protein basis, and only 20–30% in mesophyllperoxisomes. However, peroxisomes from both cell types containedsignificant levels of all the enzymes involved in the photorespiratoryglycolate pathway, when compared with castor bean glyoxysomes.The activity of hydroxypyruvate reductase in the peroxisomesof P. miliaceum was comparable to or higher than that in wheatperoxisomes. Two ß-oxidation enzymes and urate oxidasewere detected in the peroxisomes in a similar level to thatin wheat peroxisomes. These results suggest that the peroxisomes of mesophyll andbundle sheath cells of P. miliaceum are essentially similarto those of C₃ plants, and that they cannot be differentiatedexcept for a difference in equilibrium density in a sucrosegradient. (Received December 24, 1984; Accepted April 9, 1985)