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PubMed2001

[Study of the anti-icteric and hepatoprotective activity of Persea gratissima Gaertner (Lauraceae) seeds ].

The lyophilisat of Persea gratissima Gaertner almonds was administered in various quantities to eighty four rats divided in three groups of twenty eight. in the first group (negative reference group), each animal was forcefed with 5 ml of distilled water on a daily basis, in the second group (positive reference group), the rats were forcefed with 5 ml of distilled water per day, after they were intoxicated with 0,3 ml of carbon tetrachloride under cutaneous injection, in the third group (experimental animals), each animal after it was intoxicated by the same quantity of carbon tetrachloride, was forcefed on a daily basis with 14mg/100g PV of lyophilisat of avocado almonds diluted with 5 ml of distilled water. The results showed that the lyophilisat of avocado almonds have a anti-icteric activity which is reflected in the stimulation of the liver to conjugate and eliminate bilirubin, as well as hepatoprotective activity characterised by the normalisation of the aminotransferases enzymes (ASAT, ALAT) and the healing of hepatic lesions within 10 days.

Animals↗
PubMed1995

Isolation and identification of a compound from avocado (Persea americana) leaves which causes necrosis of the acinar epithelium of the lactating mammary gland and the myocardium.

It is well known that when lactating livestock eat avocado (Persea americana) leaves they may develop non-infectious mastitis and agalactia. This is associated with extensive coagulation necrosis of the secretory acinar epithelium and interstitial oedema, congestion, and haemorrhage. Similar lesions have been produced in mammary glands of lactating mice fed a diet containing a small percentage of freeze-dried avocado leaf. Tests using these animals have been used to isolate the active principle, termed "persin," from avocado leaves. The purified persin was examined using IR, NMR, and UV spectroscopy and mass spectrometry, and identified as (Z,Z)-1-(acetyloxy)-2-hydroxy-12,15-heneicosadien-4-one. Persin has previously been isolated from avocado leaves and shown to have antifungal properties and to be toxic to silkworms. Our tests have shown that persin at the dose rate of 60-100 mg/kg has the same effect on mammary glands in lactating mice as leaves from avocado. Enantioselective syntheses of the R and the S isomers of persin and related derivatives were carried out. These compounds were tested for activity required to induce widespread lactating mammary gland necrosis in mice, and only the R isomer was found active. At doses of persin above 100 mg/kg necrosis of myocardial fibres may occur and hydrothorax may be present in severely affected animals. The mechanism of action of persin on both the mammary gland and the myocardium remain to be resolved.

Animals↗
PubMed1984

N-demethylation of p-chloro-N-methylaniline catalyzed by subcellular fractions from the avocado pear (Persea americana).

Subcellular fractions from the avocado pear ( Persea americana) catalyzed formation of p-chloroaniline from p-chloro-N-methylaniline. Fractions prepared by centrifugation of avocado homogenates at 20, 000g for 20 min formed p-chloroaniline (2900 +/- 500 pmol min-1 mg protein-1) with an NADPH-generating system. p-Chloroaniline formation required reduced pyridine nucleotide (NADPH was 6-7 times more effective than NADH) and O2. N-Demethylation was inhibited by CO (55% inhibition at CO:O2 = 1) and was not inhibited by CN. Cytochrome P-450 was detected in the 20, 000g pellet at levels of 300-380 pmol/mg protein. This particulate preparation was also active in catalyzing the NADPH-dependent epoxidation of the chlorinated cyclodiene aldrin. Improvements to a colorimetric procedure for measuring p-chloroaniline increased the sensitivity of the procedure fourfold, and allowed use of samples containing high amounts of lipid. Avocado pear is suitable tissue for further studies on the oxidation of foreign compounds by higher plants.

Aniline Compounds↗
PubMed1995

Solubilisation, partial purification and properties of acyl-CoA: glycerol-3-phosphate acyltransferase from avocado (Persea americana) fruit mesocarp.

Glycerol-3-phosphate acyltransferase (G3PAT) activity was studied using a microsomal membrane fraction from avocado (Persea americana) mesocarp. G3PAT was shown to be an integral membrane protein, having an active site that appeared to be accessible to the cytoplasmic face of the endoplasmic reticulum, in experiments using limited proteolytic digestion. CHAPS solubilisation (0.25%, w/v) of microsomal G3PAT activity was used as an initial step in purification of this enzyme. Both CHAPS-solubilised and microsomal G3PAT activities were characterised and compared. Affinity chromatography was used to purify microsomal G3PAT for the first time from a plant source. Glycerophosphorylethanolamine coupled to cyanogen bromide-activated Sepharose was used for this purpose. Specific elution of G3PAT by a solution of glycerol-3-phosphate resulted in about 150-fold purification. The significance of the results and the potential usefulness of the purification method for further studies of G3PAT in plants are discussed.

Binding Sites↗
PubMed1995

A plant metabolic activation system from Persea americana with cytochrome P450-dependent and peroxidase activities.

Microsomal fractions from different tissues of various plants (potato, cauliflower, aubergine, avocado pear, courgette, cucumber, banana, kiwi and strawberry) were prepared and their content of cytochrome P-450 (cyt-P450) determined. A S117 fraction from Persea americana (avocado pear) presented the highest content of cyt-P450. As a consequence of these data, we have developed and characterized this fraction as a plant metabolic activation system. The P. americana S117, used in this work, contains 0.75 +/- 0.04 mg of protein per ml, 0.788 +/- 0.078 nmol of cyt-P450 per mg of protein and has a peroxidase activity of 0.036 +/- 0.005 (nmol tetraguaiacol/micrograms protein/min). The P. americana cyt-P450 remained stable during at least 60 days, stored at -80 degrees C. This fraction activated 2-aminofluorene to a mutagenic product in S. typhimurium TA98, while it had no effect on the benzo[a]pyrene activation. The treatment of the P. americana S117 with CO, the addition of diethyldithiocarbamate (DETC) or the absence of a NADPH-generating system in the activation mix, produced a partial inhibition of the 2-aminofluorene activation. Both peroxidase activity and a cyt-P450-dependent activity are assumed to be involved in the activation of this chemical mediated by P. americana S117.

Benzo(a)pyrene↗
PubMed1994

Cytochrome P-450-catalysed monoterpenoid oxidation in catmint (Nepeta racemosa) and avocado (Persea americana); evidence for related enzymes with different activities.

A cytochrome P-450 present in ripening avocado (Persea americana) fruit mesocarp (CYP71A1) had previously been shown to metabolize the monoterpenoids nerol and geraniol (Hallahan et al. (1992) Plant Physiol. 98, 1290-1297). Using DNA encoding CYP71A1 as a hybridization probe, we have shown by Southern analysis that a related gene is present in the catmint, Nepeta racemosa. RNA blot analysis, together with Western analysis of catmint leaf polypeptides using avocado cyt P-450 antiserum, showed that a closely related gene is expressed in catmint leaves. Cytochrome P-450 in catmint microsomes catalysed the specific hydroxylation of nerol and geraniol at C-10, whereas avocado CYP71A1, in either avocado microsomes or heterologously expressed in yeast, catalysed 2,3- or 6,7-epoxidation of these substrates. These results suggest that orthologous genes of the CYP71 family are expressed in these two plant species, but catalyse dissimilar reactions with monoterpenoid substrates.

Acyclic Monoterpenes↗
PubMed2001

Minor diterpenes from Persea indica: their antifeedant activity.

The new diterpenes anhydrocinnzeylanone, garajonone and 2,3-didehydrocinnzeylanone, and the known anhydrocinnzeylanine, have been isolated from Persea indica. The antifeedant activity of these compounds has been evaluated showing the importance of the 11-hemiketal group for the antifeedant effects of ryanodane diterpenes.

Animals↗
PubMed1998

Additional cytotoxic neolignans from Persea obovatifolia.

Four additional neolignans, comprising obovatifol [(2S,3S)-2,3-dihydro-2- (3,4-dihydroxy-5-methoxyphenyl)-7-methoxy-3-methyl-5-trans-propenyl benzofuran], obovaten [2-(3,4-dihydroxy-5-methoxyphenyl)-7-methoxy-3- methyl-5-trans-propenyl benzofuran], perseal C [(2S,3R)-2,3-dihydro-2-(3,4-methylenedioxyphenyl)-5- formyl-3-hydroxymethyl-7-methoxy benzofuran] and perseal D [2-(3,4-dihydroxy-5-methoxyphenyl)-5-formyl-7- methoxy-3-methyl benzofuran] were isolated in a continuing study of the leaves of Persea obovatifolia. Obovatifol had been reported previously in a mass spectrometric analysis without any other spectroscopic data. Obovaten and perseals C and D are new compounds, bearing a C-1' formyl side-chain, instead of a propenyl group. Their structures were elucidated from spectroscopic data; they showed significant cytotoxic activities against P-388, KB16, A549 and HT-29 cancer cell lines in vitro.

Animals↗
PubMed2001

Antibacterial activity of Persea cordata stem barks.

The antibacterial effects of extracts obtained from Persea cordata stem bark, employed in Brazil to treat infectious diseases, were studied. The ethyl acetate fraction of the hydroalcoholic extract showed activity against pathogenic bacteria which may justify the popular use of the plant.

Bacteria↗
PubMed2002

Analgesic and anti-inflammatory effects of the aqueous extract of leaves of Persea americana mill (lauraceae).

The aqueous extract of Persea americana leaves produced a dose-dependent inhibition of both phases of formalin pain test in mice, a reduction in mouse writhing induced by acetic acid and an elevation of pain threshold in the hot plate test in mice. The extract also produced a dose-dependent inhibition of carrageenan-induced rat paw oedema. The results obtained indicate that the extract possesses analgesic and anti-inflammatory effects.

Analgesics↗
PubMedDate not supplied

Majorenolide and majorynolide: a new pair of cytotoxic and pesticidal alkene-alkyne delta-lactones from Persea major.

From the EtOH extract of the bark of Persea major, two bioactive compounds, majorynolide [1] and majorenolide [2], were isolated by activity-directed fractionation using brine shrimp. Their structures have been elucidated on the basis of spectral data as a pair of new alkene-alkyne delta-lactones, each with an exocyclic alkylidene methine carbon. Both 1 and 2 are moderately cytotoxic, and 2 is selectively pesticidal.

Animals↗
PubMed1998

Cytotoxic and insecticidal constituents of the unripe fruit of Persea americana.

Unripe avocado fruit (Persea americana) was subjected to a bioactivity-directed fractionation, as monitored via the brine shrimp lethality assay, to isolate three major bioactive constituents (1-3). Compounds 1-3 all have a 1,2,4-triol moiety and a long aliphatic chain that terminates as either an alkane, alkene, or alkyne, respectively; 1 is new, while 2 and 3 have been described previously but not as cytotoxic or pesticidal agents. All have activity against six human tumor cell lines in culture and show selectivity for human prostate adenocarcinoma (PC-3) cells with 3 being nearly as potent as adriamycin. Also, when tested against yellow fever mosquito larva, 3 was more effective than rotenone, a natural botanical insecticide and positive control.

Aedes↗
PubMed2001

Purification and catalytic properties of polygalacturonase isoforms from ripe avocado (Persea americana) fruit mesocarp.

Endo-polygalacturonase (PG; EC 3.2.1.15) was recovered from the cell walls of avocado mesocarp (Persea americana Mill cv. Lula) tissue and purified by sequential ion exchange and gel permeation chromatography. Two isoforms (S-I and S-II) were recovered, exhibiting molecular masses of about 41 kD on size exclusion media and about 48 (S-I) and 46 (S-II) kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Both isoforms exhibited maximum activity at pH 6.0 against polygalacturonic acid (PGA) and hydrolyzed PGA of about 180 kDa to polymers of about 4 kDa. The catalytic activity of the 48-kDa isoform against PGA was slightly higher than that of the 46-kDa isoform. The purified PGs catalyzed significant molecular mass downshifts in the polyuronides of pre-ripe avocados; however, the capacity of the enzymes to solubilize polyuronides from cell walls of pre-ripe fruit was limited.

Journal Article↗
PubMed1980

Acetyl-coenzyme A carboxylase from avocado (Persea americana) plastids and spinach (Spinacia oleracea) chloroplasts.

Preparations of acetyl-CoA carboxylase [acetyl-CoA-carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] have been obtained from the plastids of avocado (Persea americana) fruit mesocarp and from spinach (Spinacia oleracea) chloroplasts. Both preparations required bovine serum albumin, HCO3-, citrate and glycerol for stabilization. The molecular weight of the avocado enzyme was about 6.5 X 10(5) on the basis of 1 mol of biotin/mol of enzyme, the behaviour of both enzymes on gel filtration being in accord with such a value. Removal of the stabilizing bovine serum albumin resulted in the loss of a biotin-containing fragment from the avocado enzyme. Citrate stabilized the enzyme at 10 mM and activated it optimally at 3.0 mM, effecting an approx. 2-fold increase in Vmax. It is suggested that in vivo the enzyme may be located within the chloroplast lamellae.

Acetyl-CoA Carboxylase↗
PubMed1990

3-Oxoacyl-(acyl-carrier protein) reductase from avocado (Persea americana) fruit mesocarp.

The NADPH-linked 3-oxoacyl-(acyl-carrier protein) (ACP) reductase (EC 1.1.1.100), also known as 'beta-ketoacyl-ACP reductase', has been purified from the mesocarp of mature avocado pears (Persea americana). The enzyme is inactivated by low ionic strength and low temperature. On SDS/PAGE under reducing conditions, purified 3-oxoacyl-ACP reductase migrated as a single polypeptide giving a molecular mass of 28 kDa. Gel-filtration chromatography gave an apparent native molecular mass of 130 kDa, suggesting that the enzyme is tetrameric. The enzyme is inactivated by dilution, but some protection is afforded by the presence of NADPH. Kinetic constants have been determined using synthetic analogues as well as the natural ACP substrate. It exhibits a broad pH optimum around neutrality. Phenylglyoxal inactivates the enzyme, and partial protection is given by 1 mM-NADPH. Antibodies have been raised against the protein, which were used to localize it using immunogold electron microscopy. It is localized in plastids. N-Terminal amino-acid-sequence analysis was performed on the enzyme, and it shows close structural similarity with cytochrome f. Internal amino-acid-sequence data, derived from tryptic peptides, shows similarity with the putative gene products encoded by the nodG gene from the nitrogen-fixing bacterium Rhizobium meliloti and the gra III act III genes from Streptomyces spp.

3-Oxoacyl-(Acyl-Carrier-Protein) Reductase↗
PubMed1992

Carbon dioxide exchange of developing avocado (Persea americana Mill.) fruit.

Net efflux of CO(2) from attached avocado (Persea americana Mill.) fruit was measured periodically from three weeks after anthesis to fruit maturity. Net CO(2) exchange was determined in daylight (light respiration, R(l)) at a photosynthetic photon flux (PPF) greater than 600 micromol m(-1) s(-1), and in the dark (dark respiration, R(d)). Dark respiration and R(l) were highest during the early cell division stage of fruit growth (about 25 and 22 nmol CO(2) g(dw) (-1) s(-1), respectively) and decreased gradually until fruit maturity to about 1 and 0.5 nmol CO(2) nmol CO(2) g(dw) (-1) s(-1), respectively. Fruit photosynthesis, calculated from the difference between R(d) and R(l), ranged from 0.5 to 3.1 nmol CO(2) g(dw) (-1) s(-1). Net rate of CO(2) assimilation on a fruit dry weight basis was highest during the early stages of fruit growth and reached the lowest rate at fruit maturity. Net rate of CO(2) assimilation of fruit exposed to light was 0.4 to 2.5% of that for fully expanded leaves. Although the relative amount of carbon assimilated by the fruit was small compared with the total amount of carbon assimilated by the leaves, the data indicate that avocado fruit contribute to their own carbon requirement by means of CO(2) assimilated in the light.

Journal Article↗
PubMed1994

Partitioning of photoassimilates in avocado (Persea americana Mill.) during flowering and fruit set.

To assess competition for photoassimilates among developing inflorescences, fruitlets and vegetative shoots in avocado (Persea americana Mill.), the distribution of recent photoassimilates was examined before and during flowering, fruit set, and the transition from sink to source of developing vegetative shoots. Mature leaves, located proximal to developing reproductive organs, and developing leaves, located distal to those organs, were exposed to a one-hour pulse of (14)CO(2). Translocation of radiolabeled assimilates was monitored over time and among organs. Overall distribution of assimilates was dependent on dry mass of tissues regardless of organ type. Flowers and fruitlets did not demonstrate greater sink strength than non-autotrophic leaves. Organs receiving assimilates were in phyllotactic alignment with source leaves. Photoassimilates were never limiting, although flower and fruitlet abscission occurred during and long after this competitive period. Carbohydrate availability was sufficient to support the growth of both developing fruitlets and leaves during early stages of reproductive development, and it did not limit fruitlet growth or stimulate fruitlet abscission.

Journal Article↗