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1.
On the Mechanism of the Changes in Phenylalanine Ammonia-lyase Activity Induced by Ultraviolet and Blue Light in Gherkin Hypocotyls 总被引:5,自引:1,他引:4
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Engelsma G 《Plant physiology》1974,54(5):702-705
Irradiation with ultraviolet light causes in the hypocotyl of dark-grown gherkin seedlings the partial conversion of trans-hydroxycinnamic acids to the cis-isomers. The trans-hydroxycinnamic acids inhibit the development of phenylalanine ammonia-lyase activity, and the transformation of these compounds to the much less inhibitory cis-isomers forms a ready explanation for the increase in phenylalanine ammonia-lyase activity in the hypocotyl of gherkin seedlings irradiated with ultraviolet light. Arguments are advanced that the increase in phenylalanine ammonia-lyase activity caused by irradiation with blue light is also (at least in part) initiated by trans-cis isomerisation of the hydroxycinnamic acids. 相似文献
2.
Blue light mediates a transient increase in the extractable activity of phenylalanine ammonia-lyase from both cotyledons and hypocotyls of etiolated gherkin seedlings, but concurrent changes in extractable cinnamic acid 4-hydroxylase activity only occur in cotyledons. Excision, followed by incubation in the dark, also results in stimulation of the lyase activity in both tissues, but the hydroxylase activity is only stimulated in cotyledons, again concurrently with the lyase. Stimulated levels of hydroxycinnamic acid esters are, however, only formed following light treatment, indicating the presence of another light-sensitive step in their biosynthesis. Treatment of gherkin tissues with 2-aminooxyacetic acid or α-aminooxy-β-phenylpropionic acid inhibits phenylalanine ammonia-lyase activity in situ, reduces the accumulation of hydroxycinnamic acid esters and presumably reduces the endogenous cinnamic acid pool. This treatment increases extractable lyase activity and delays its peak in activity. In cotyledons, these changes in the lyase are associated with concurrent and similar changes in extractable hydroxylase activity, whilst in hypocotyls the hydroxylase is relatively unaffacted. The increase in phenylalanine ammonia-lyase activity following excision of cotyledons and hypocotyls is prevented by cinnamic acid; in cotyledons the hydroxylase is similarly affected, but after a longer lag. Thus whilst cinnamic acid can modify the extractable activity of the lyase, it cannot itself mediate changes in the extractable activity of the hydroxylase. 相似文献
3.
Terry H. Attridge Harry Smith 《Biochimica et Biophysica Acta (BBA)/General Subjects》1974,343(3):452-464
Evidence is presented which demonstrates that both acid phosphatase (EC 3.1.3.2) and phenylalanine ammonia-lyase (EC 4.3.1.5) are synthesised in the hypocotyls of dark-grown gherkin seedlings. When blue light or cycloheximide treatment is given in the presence of 2H2 O the buoyant density of the lyase is observed to be lower than the appropriate dark control. This effect is not found for the phosphatase, the buoyant density of which is unaffected by blue ligh. These data appear to be best interpreted as a blue-light- and cycloheximide-mediated activation of previously synthesised, inactivated phenylalanine ammonia-lyase. 相似文献
4.
5.
The extractable activity of L-phenylalanine ammonia-lyase (EC 4.3.1.5) and the concentration of sugar esters of p-coumaric and ferulic acids in the hypocotyls of etiolated gherkin seedlings increase upon irradiation with white light. Treatment of intact seedlings with the phenylalanine ammonia-lyase inhibitors alpha-aminooxyacetic acid and L-alpha-aminooxy-beta-phenylpropionic acid during illumination causes enhanced formation of the lyase and reduces the accumulation of hydroxycinnamic acids. Enzyme activity in excised hypocotyl segments floating on buffer increases in the dark as well as in the light, while hydroxycinnamic acids accumulate only in the light. Phenylalanine ammonia-lyase formation in the segments is inhibited by cinnamic acid and, to a lesser extent, p-coumaric acid, while it is slightly enhanced by caffeic acid and is not affected by ferulic acid. Aminooxyphenylpropionate dramatically promotes phenylalanine ammonia-lyase formation in the segments in darkness and light prevents the accumulation of hydroxycinnamic acids in the light. Aminooxyphenylpropionate does not, however, affect the time course of apparent lyase formation and decay. Cinnamic acid, the product of the lyase reaction, antagonizes the effect of aminooxyphenylpropionate. It is proposed that the reaction product(s) are involved to some extent in the regulation of the pool of active lyase in the hypocotyl tissue. 相似文献
6.
Nikolaus Amrhein Jürgen Gerhardt 《Biochimica et Biophysica Acta (BBA)/General Subjects》1979,583(4):434-442
The extractable activity of l-phenylalanine ammonia-lyase (EC 4.3.1.5) and the concentration of sugar esters of p-coumaric and ferulic acids in the hypocotyls of etiolated gherkin seedlings increase upon irradiation with white light. Treatment of intact seedlings with the phenylalanine ammonia-lyase inhibitors α-aminooxyacetic acid and l-α-aminooxy-β-phenylpropionic acid during illumination causes enhanced formation of the lyase and reduces the accumulation of hydroxycinnamic acids. Enzyme activity in excised hypocotyl segments floating on buffer increases in the dark as well as in the light, while hydroxycinnamic acids accumulate only in the light. Phenylalanine ammonia-lyase formation in the segments is inhibited by cinnamic acid and, to a lesser extent, p-coumaric acid, while it is slightly enhanced by caffeic acid and is not affected by ferulic acid.Aminooxyphenylpropionate dramatically promotes phenylalanine ammonialyase formation in the segments in darkness and light and prevents the accumulation of hydroxycinnamic acids in the light. Aminooxyphenylpropionate does not, however, affect the time course of apparent lyase formation and decay. Cinnamic acid, the product of the lyase reaction, antagonizes the effect of aminooxyphenylpropionate. It is proposed that the reaction product(s) are involved to some extent in the regulation of the pool of actively lyase in the hypocotyl tissue. 相似文献
7.
A specific and reversible macromolecular inhibitor of phenylalanine ammonia-lyase and cinnamic acid-4-hydroxylase in gherkins 总被引:2,自引:0,他引:2
A non-dialysable inhibitor of phenylalanine ammonia-lyase (L-phenylalanine ammonia-lyase, EC 4.3.1.5) has been partially purified from dark-grown gherkin hypocotyls. On extraction of tissue it is found both in the soluble (106 000 X g supernatant) and microsomal (106 000 X g pellet) fractions and can be extracted from the microsomal membranes with 10 mM sodium cholate and 1 M KCl. The soluble and microsomal fractions have similar properties, suggesting the presence of the same active component. The inhibitor is small (Mr less than 20 000), thermolabile, sensitive to proteolytic digestion, and apparently hydrophobic. Purification of the inhibitor was achieved by chromatography on DEAE-cellulose by gel filtration on Sephadex G-50. The inhibitor preparations inhibit phenylalanine ammonia-lyase isolated from a number of plant tissues and also cinnamic acid-4-hydroxylase (trans-cinnamate, NADPH:oxygen oxidoreductase (4-hydroxylating), EC 1.14.13.11) from gherkins and peas, but not a wide range of other enzymes. The evidence suggests that inhibition of the two enzymes is due to the same substance, but this has not yet been confirmed. Kinetic experiments show that the inhibitor is competitive with phenylalanine for the lyase and that its association with the lyase is reversible. Further, a mixture of inhibitor and lyase can be separated on non-denaturing polyacrylamide gels without loss of lyase activity. The activities of phenylalanine ammonia-lyase and cinnamic acid 4-hydroxylase are often concurrently regulated and both have regulatory roles in phenol metabolism; it is suggested that the inhibitor may be specifically involved in controlling their activities in vivo. 相似文献
8.
C. J. LAMB 《Plant, cell & environment》1982,5(6):471-475
Abstract The accumulation of chlorogenic acid in illuminated discs of Solanum tuberosum tuber tissue is accompanied by rapid but transient increases in the activity levels of the biosynthetic enzymes phenylalanine ammonia-lyase, cinnamic acid 4-hydroxylase and hydroxycinnamoyl-CoA : quinate hydroxycinna-moyl transferase. Exogenous D-phenylalanine and L-α-aminooxy-β-phenylpropionic acid, competitive inhibitors of phenylalanine ammonia-lyase, inhibit the accumulation of chlorogenic acid and presumably reduce the endogenous pools of pathway intermediates such as cinnamic acid. These treatments prolong the phase of increase in phenylalanine ammonia-lyase and cinnamic acid 4-hydroxylase activities and indicate that product feedback modulation is important in maintaining the interrelationship between the levels of these two enzymes during the later stages of induction. In contrast,L-α-aminooxy-β-phenylpropionic acid inhibits the development of hydroxycinnamoyl transferase in illuminated discs supporting the idea that the light-stimulated increase in phenylalanine ammonia-lyase activity causes an increase in cinnamic acid production which mediates the light-stimulated increase in hydroxycinnamoyl transferase activity. 相似文献
9.
Ethylene-enhanced Synthesis of Phenylalanine Ammonia-Lyase in Pea Seedlings 总被引:12,自引:10,他引:2
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The effect of ethylene on the development of phenylalanine ammonia-lyase activity in segments excised from the epicotyl apex of pea seedling was studied. Although there was some increase in phenylalanine ammonia-lyase activity in segments not treated with ethylene, a marked increase in phenylalanine ammonia-lyase activity occurred in ethylene-treated tissues during the incubation. The induction period was estimated to be about 6 hours. The activity reached a maxmum at 30 hours and then declined. On withdrawal of ethylene, the increase was sustained for a short period and then stopped. After retreatment with ethylene, the increase was resumed. Addition of CO2 reduced the effect of ethylene. Administration of cycloheximide or actinomycin D at an early period almost completely suppressed the increase in phenylalanine ammonia-lyase activity. However, if these inhibitors were administered at a later period, while phenylalanine ammonia-lyase activity was approaching a maximum, they not only failed to reduce but rather stimulated the activity. These results are consistent with the view that there exist both phenylalanine ammonia-lyase-synthesizing and -inactivating systems, and that the development of both systems may involve de novo synthesis of protein. 相似文献
10.
Terry H. Attridge Christopher B. Johnson Harry Smith 《Biochimica et Biophysica Acta (BBA)/General Subjects》1974,343(3):440-451
When dark-grown mustard seedlings are irradiated with far-red light the level of phenylalanine ammonia-lyase (EC 4.3.1.5) activity increases. After 2H2 O treatment phynlalanine amonia-lyase from seedlings irradiated with far-red light is density-labelled to a lesser extent than enzyme from dark-grown tissue. Theoretical arguments are advanced and data presented which show that this result cannot be explained in terms of an increase in de novo synthesis of phenylalanine ammonia-lyase and that the increase most likely involves activation of existing enzyme. 相似文献
11.
Summary A procedure is described which permits the estimation of the relative activity of phenylalanine ammonia-lyase (E.C. 4.3.1.5.) in intact plant cells, exemplified by buckwheat hypocotyls. Hypocotyl segments are incubated at pH 5.5 with L-[3-3H]phenylalanine. N3HH2, which is liberated from phenylalanine by the action of phenylalanine ammonia-lyase, equilibrates with tissue water to yield 3HOH, which is recovered by sublimation. Participation of phenylalanine transaminase in the reactions leading to 3HOH formation is excluded, and it is conclusively shown that 3HOH is formed intracellularly and not by enzymatic activity leaking out of wounded tissue.Abbreviation PAL
phenylalanine ammonia-lyase (E.C. 4.3.1.5.) 相似文献
12.
The purification of phenylalanine ammonia-lyase (PAL) from S. pararoseus is described: PAL is recovered from cellular extracts by acid precipitation of contaminating proteins, nucleic acids and carotenoids; concentrated by ultrafiltration and purified by ion exchange chromatography in DEAE-Sephacel, with 80% yield and 32.6 fold purification. Elimination of carotenoids and stabilization with glycerol are introduced in the methodology to increase stability and purification yield. 相似文献
13.
Peltonen Sari Mannonen Leena Karjalainen Reijo 《Plant Cell, Tissue and Organ Culture》1997,50(3):185-193
Suspension-cultured barley cells responded to treatments with crude yeast extract and purified glucan preparation by rapidly
and transiently (4 h postelicitation) inducing L-phenylalanine ammonia-lyase activity. Similarly, treatment of cell cultures
with chitosan resulted in increased phenylalanine ammonia-lyase activity 2–4 h after elicitation, whereas a mycelium preparation
of a fungal pathogen, Bipolaris sorokiniana, and purified chitin caused a more delayed induction of phenylalanine ammonia-lyase
(8 h postelicitation). The most abundant of the plant cell wall degrading enzymes produced by Bipolaris sorokiniana, β-1,4-xylanase,
had only a weak elicitor activity in barley cells suggesting that fungal cell wall components rather than the hydrolytic enzymes
secreted by the fungus function as recognizable components that cause barley cells to induce defences. Treatment of the elicited
cells with a phenylalanine ammonia-lyase inhibitor, α-aminooxy-β-phenylpropionic acid, resulted in the superinduction of the
enzyme indicating the blocking of the feedback regulation mechanisms, whereas in the presence of 1 mM trans-cinnamic acid
the elicitor-induction of phenylalanine ammonia-lyase was completely inhibited. Elicitor treatments increased the accumulation
of wall-bound phenolics as evidenced by phloroglucinol-HCl staining and thioglycolic acid methods. However, α-aminooxy-β-phenylpropionic
acid applied in combination with the elicitor did not prevent the accumulation of phenolics in barley cell walls. This suggested
that phenylalanine ammonia-lyase might not play an important role in the synthesis wall-bound phenolic compounds in barley.
However, cinnamic acid, whether applied alone or together with the elicitor, increased the amount of wall-bound phenolics
in suspension-cultured barley cells.
This revised version was published online in June 2006 with corrections to the Cover Date. 相似文献
14.
G P Bolwell J N Bell C L Cramer W Schuch C J Lamb R A Dixon 《European journal of biochemistry》1985,149(2):411-419
L-Phenylalanine ammonia-lyase (EC 4.3.1.5) has been purified over 200-fold from cell cultures of bean (phaseolus vulgaris L.) exposed to elicitor heat-released from the cell walls of the phytopathogenic fungus Colletotrichum lindemuthianum. Four forms of the enzyme, with identical Mr but differing apparent pI values of 5.4, 5.2, 5.05 and 4.85, were observed following the final chromatofocussing stage of the purification. A preparation (purified 43-fold by ammonium sulphate precipitation, gel-filtration and ion-exchange chromatography) containing all four forms exhibited apparent negative rate cooperativity with respect to substrates. However, the individual forms displayed normal Michaelis-Menten kinetics, with Km values of 0.077 mM, 0.122 mM, 0.256 mM and 0.302 mM in order of decreasing apparent pI value. A preparation purified 200-fold and containing all four forms was used to immunise rabbits for the production of anti-(phenylalanine ammonia-lyase) serum. The antiserum was characterised by: immunotitration experiments; solid phase enzyme-linked immunosorbent assays; comparison of immunoprecipitates of 35S-labelled phenylalanine ammonia-lyase subunits (synthesized both in vivo and in vitro) on both one-dimensional and two-dimensional polyacrylamide gels after immunoprecipitation with the bean antiserum or antisera raised against pea and parsley phenylalanine ammonia-lyase preparations and immune blotting. SDS/polyacrylamide gels and SDS/polyacrylamide gel electrophoresis followed by immune blotting, indicated that the Mr of newly synthesized (in vivo and in vitro) bean phenylalanine ammonia-lyase subunits is 77000; a 70000-Mr form is readily generated as a partial degradation product during purification. Immunoprecipitates of bean phenylalanine ammonia-lyase synthesized both in vivo and in vitro showed the presence of multiple subunit types of identical Mr but differing in pI. Furthermore, treatment of bean cultures with Colletotrichum elicitor resulted in a 10-fold increase in phenylalanine ammonia-lyase extractable activity within 8 h, and chromatofocussing analysis indicated that this was associated with differential increased appearance of the high-pI, low-Km forms as compared to the two higher Km forms. This differential induction was further confirmed by immune blotting of crude extracts subjected to isoelectric focussing. 相似文献
15.
Circadian Rhythmicity in the Activities of Phenylalanine Ammonia-Lyase from Lemna perpusilla and Spirodela polyrhiza
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The oscillations in phenylalanine ammonia-lyase activity from Spirodela polyrhiza and phenylalanine ammonia-lyase and tyrosine ammonia-lyase activities from Lemna perpusilla displayed a circadian rhythm under continuous light. Rhythmicity in enzymic activity could not be detected in continuous darkness since under this condition phenylalanine ammonia-lyase activity remains at a fairly constantly low level. Results from our studies of the oscillatory pattern of the respective activities of phenylalanine and tyrosine ammonia-lyase support their “inseparability.” 相似文献
16.
Wound-induced phenylalanine ammonia-lyase in potato (Solanum tuberosum) tuber discs. Significance of glycosylation and immunolocalization of enzyme subunits. 总被引:3,自引:0,他引:3
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1. Excised discs of potato (Solanum tuberosum) tuber were incubated with [3H]fucose and extracts were prepared and incubated with an antibody to phenylalanine ammonia-lyase. Analysis of the resulting immunoprecipitated proteins by SDS/PAGE showed [3H]mannose- and [3H]fucose-labelled bands with Mr values corresponding to those of phenylalanine ammonia-lyase subunits. 2. When potato discs were incubated with [3H]sugars in the presence of tunicamycin, an inhibitor of N-linked protein glycosylation, incorporation of radioactivity from [3H]mannose into the immunoprecipitated enzyme subunits was virtually eliminated, whereas that from [3H]fucose was only marginally inhibited. 3. Tunicamycin reduced the level of extractable phenylalanine ammonia-lyase activity induced in excised potato tuber discs. Kinetic analysis revealed that the Vmax value of the enzyme in crude extracts from tunicamycin-treated tissue was reduced, whereas the apparent Km values were unaffected. 4. Immunoprecipitation of the enzyme labelled in vivo with [35S]methionine showed that tunicamycin did not inhibit the synthesis of the enzyme protein per se, nor did it increase the degradation of the enzyme protein. 5. Immunoprecipitation of the enzyme labelled in vitro with [14C]nitromethane showed that tunicamycin did not affect the introduction of the dehydroalanine residue into the active site. 6. These results are consistent with the following hypothesis: tunicamycin inhibits the N-linked glycosylation of phenylalanine ammonia-lyase which, in turn, results in imperfect folding of the enzyme protein. The orientation of the active site is changed in such a way that the affinity of the enzyme for its substrate is unaffected, whereas the catalytic activity of the enzyme is reduced. 7. Both optical- and electron-microscopic immunolocalization studies with antibody to phenylalanine ammonia-lyase showed increased deposition of silver granules in cells in sections of potato discs in which induction of the enzyme was allowed to occur compared with cells from newly wounded tissue. The enzyme was located in the cytoplasm, and was possibly membrane-associated. 相似文献
17.
Summary To determine whether phenylalanine ammonia-lyase (EC 4.3.1.5) is involved in the maturation of microspores to fertile pollen, anthers of a fertile strain of broccoli (Brassica oleracea L.) were studied in a comparison with anthers of a cytoplasmic male sterile strain. In the normal fertile strain, immature anthers of about 2 mm in length exhibited higher phenylalanine ammonia-lyase activity than mature anthers or those shorter than 2 mm. The 2-mm-long anthers corresponded to the mononucleate stage, just after release of the microspores during pollen development. Immunohistochemical localization of phenylalanine ammonia-lyase in the anthers indicated that the protein was present predominantly in the tapetal cells. The immature anthers of cytoplasmic male sterile broccoli had a lower phenylalanine ammonia-lyase activity than those of the normal fertile strain. The level of phenylalanine ammonia-lyase activity in the immature anthers was positively correlated with the number of fertile pollen grains at the flowering stage in both strains. It seems possible, therefore, that phenylpropanoid metabolism, which involves phenylalanine ammonia-lyase, may play an important role in the maturation of microspores in flowering plants.Abbreviations CHS
chalcone synthase
- CMS
cytoplasmic male sterility
- DAPI
4, 6-diamidmo-2-phenylindole dihydrochloride
- PAL
L-phenylalanine ammonia-lyase 相似文献
18.
Differential response of cultured parsley cells to elicitors from two non-pathogenic strains of fungi. 2. Effects on enzyme activities 总被引:4,自引:0,他引:4
Parsley cell cultures produce linear furanocoumarins and the linear benzodipyrandione, graveolone, in response to treatment with an elicitor from either Phytophthora megasperma or Alternaria carthami. Activities of enzymes involved in general phenylpropanoid metabolism, phenylalanine ammonia-lyase and 4-coumarate: CoA ligase, as well as of an enzyme involved specifically in furanocoumarin biosynthesis, dimethylallyl diphosphate: umbelliferone dimethylallyltransferase, were monitored over several days after treatment with A. carthami elicitor. In addition, the activities of chalcone synthase, an enzyme involved in flavonoid formation, and of glucose-6-phosphate: NADP 1-oxidoreductase were also monitored. The lyase and the ligase activities increased steadily for 48 h and the dimethylallyltransferase activity for 54 h, while the synthase activity was not altered and the oxidoreductase activity decreased gradually. In some experiments, phenylalanine ammonia-lyase activity reached a maximum value of 250 mukat/kg, twice the maximal activity observed previously in parsley cells after treatment with either ultraviolet light or an elicitor preparation from P. megasperma. In crude extracts, phenylalanine ammonia-lyase activity was shown to be inhibited by unidentified small-molecular-weight compounds which were formed in proportion to the elicitor treatment. While phenylalanine ammonia-lyase and dimethylallyl diphosphate: umbelliferone dimethylallyltransferase are known to be required for furanocoumarin biosynthesis, the involvement of 4-coumarate: CoA ligase is as yet unclear. The concomitant increase and decrease of the ligase activity with the activities of the lyase and the dimethylallyltransferase, as well as its similar response to elicitor concentrations, suggest that CoA esters of cinnamic acids play a role in the biosynthesis of furanocoumarins. 相似文献
19.
The appearance of phenylalanine ammonia-lyase activity and the accumulation of chlorogenic acid in potato tuber discs are stimulated by illumination with white light, whereas the appearance of cinnamic acid 4-hydroxylase activity is unaffected by illumination. The photosensitive step in chlorogenic acid biosynthesis may be by-passed by treatment of discs with exogenous supplies of cinnamic acid, whereas treatment of discs with phenylalanine does not isolate the photosensitive step. Therefore, the site of photocontrol of chlorogenic acid biosynthesis in potato tuber discs is the reaction catalysed by phenylalanine ammonia-lyase. Cinnamic acid 4-hydroxylase activity in vitro is unaffected by p-coumaric acid, caffeic acid or chlorogenic acid. Phenylalanine ammonia-lyase activity in vitro is sensitive to inhibition by cinnamic acid. The in vitro properties of the two enzymes are also consistent with the hypothesis that phenylalanine ammonia-lyase rather than cinnamic acid 4-hydroxylase is important in the regulation of chlorogenic acid biosynthesis in potato tuber discs. 相似文献
20.
1. Cooperation between phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) and cinnamic acid hydroxylases was investigated using microsomal fractions from cotyledons of cucumber (Cucumis sativus L.). The interpretations were based on experiments which demonstrate a limited exchange between the pool of cinnamic acid formed by the membrane-bound phenylalanine ammonia-lyase and the cinnamic acid pool external to the enzyme-membrane system. 2. The extent of cooperation between the microsomal enzymes was proved to be influenced by treatment of the cotyledons with light. On exposure to UV-light, which is known to enhance greatly the soluble phenylalanine ammonia-lyase activity in cell cultures, differential effects on the levels of microsomal and soluble phenylalanine ammonia-lyase, and of cinnamic acid hydroxylases, were observed. The time course of the enzyme activities and their cooperation in vitro after treatment of the cotyledons with light were studied. 3. The extent of cooperation in vitro was found to vary depending on the concentration of L-phenylalanine. 4. Homogenates obtained from etiolated cotyledons of Cucumis sativus in the absence of Mg2+ were fractionated by sucrose density gradient centrifugation and examined for phenylalanine ammonia-lyase, cinnamic acid o-hydroxylase, cinnamic acid o-hydroxylase, and several marker enzymes. Ammonia-lyase activity was highest in fractions with 25% sucrose, in which primarily smooth endoplasmic reticulum is localized. Hydroxylase activities co-occur with phenylalanine ammonia-lyase in these fractions (density=1.100 g/cm3), and also in fractions at higher densities (d=1.12–1.13 and 1.15 g/cm3).Abbreviations PAL
L-phenylalanine ammonia-lyase
- Tris
tris-(hydroxymethyl)aminomethane
- EDTA
ethylenediamine tetraacetic acid
- ATPase
ATP phosphohydrolase 相似文献