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1.
Braz J Biol ; 83: e274260, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38422259

RESUMO

Several studies have been carried out to expand the use of Ricinus communis L. castor bean (Ricinus communis L castor bean.). This oilseed finds appropriate conditions for its development in Brazil, with more than 700 applications. The main allergens of this plant are Ric c1 and Ric c3, that cross-react with various aeroallergens and food allergens such as peanuts, soybeans, corn, and wheat. This study aimed to determine the effect of mutations in Ric c3 amino acid residues known to affect IgE binding and allergy challenges. Based on the Ric c3 structure, B-cell epitopes, and amino acid involved in IgE binding, we produce recombinant mutant protein, mrRic c3, secreted from E. coli. Strategic glutamic acid residues in IgE-biding regions were changed by Leucine. The allergenicity of mrRic c3 was evaluated by determination of IgE, IgG1, and total IgG in immunized Balb/c mice and by degranulation assays of mast cells isolated from Wistar rats. The mrRic c3 presented a percentage of mast cell degranulation close to that seen in the negative control, and the immunization of mice with mrRic c3 presented lower levels of IgE and IgG1 than the group treated with the protein without mutations. The mutant mrRic c3 had an altered structure and reduced ability to stimulate pro-inflammatory responses and bind IgE but retained its ability to induce blocking antibodies. Thus, producing a hypoallergenic mutant allergen (mrRic c3) may be essential in developing new AIT strategies.


Assuntos
Alérgenos , Escherichia coli , Ratos , Camundongos , Animais , Alérgenos/química , Alérgenos/genética , Escherichia coli/genética , Imunoglobulina E , Ratos Wistar , Proteínas Recombinantes , Imunoglobulina G , Aminoácidos
2.
Int J Biol Macromol ; 113: 821-828, 2018 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-29522821

RESUMO

Castor cake is a by-product of the extraction of oil from from seeds of castor plants (Ricinus communis). This by-product contains high levels of proteins, but a toxic protein, ricin, limits its use as an animal feed. Ricin can be efficiently inactivated by treatment with calcium oxide (CaO), which can be evaluated by a cytotoxicity assay using LLC-MK2 cells. The mechanism by which the CaO treatment inactivates ricin, however, is unclear. We report the structural changes responsible for ricin inactivation. Purified ricin was treated with 0.6% CaO and then analyzed by mass spectrometry. This treatment degraded the ricin at preferential sites. The aqueous CaO solution had a pH >12, which preferentially cleaved asparagine residues, followed by glutamine, serine and glycine residues. The alkaline pH affected the tertiary structure of the ricin, cleaving its polypeptide chains and thereby eliminating its cytotoxic activity.


Assuntos
Citotoxinas/toxicidade , Ricina/toxicidade , Animais , Compostos de Cálcio/farmacologia , Linhagem Celular , Óxidos/farmacologia , Proteômica , Ricina/antagonistas & inibidores
3.
Genet Mol Res ; 15(4)2016 Oct 24.
Artigo em Inglês | MEDLINE | ID: mdl-27813588

RESUMO

Coffee, an agronomical crop of great economic importance, is also among the most commonly traded commodities in worldwide markets. Antimicrobial peptides, which play a role in plant defense, have been identified and isolated particularly from seeds. We isolated and immunolocalized Cc-LTP2, a new lipid transfer protein (LTP) from Coffea canephora seeds. We report its antimicrobial activity against various phytopathogenic fungi of economic importance, and against the bacterium Xanthomonas euvesicatoria. Peptides from C. canephora seeds were initially extracted using acid buffer and subjected to ion-exchange and reverse-phase chromatographies. A purified peptide of approximately 9 kDa, which we named Cc-LTP2, was then subjected to amino acid sequencing. The analyses showed that it was similar to LTPs isolated from various plants. The tissue and subcellular localization of C. canephora LTPs indicated that they were located in cell walls and intracellular palisade parenchyma, mainly in large vacuoles. The results of immunohistochemistry and histochemistry superposed from C. canephora seed tissues showed that LTPs and lipid bodies are present in organelles, supporting the hypothesis that LTPs from seeds are involved in lipid mobilization during germination. Cc-LTP2 did inhibit the development of the phytopathogenic fungi Colletotrichum lindemuthianum, Colletotrichum gloeosporioides, Fusarium solani, Fusarium lateritium, and Colletotrichum sp, but did inhibit X. euvesicatoria. Cc-LTP2 also increased membrane permeability and induced endogenous production of reactive oxygen species in all the fungi tested.


Assuntos
Anti-Infecciosos/química , Antifúngicos/química , Proteínas de Transporte/química , Coffea/química , Anti-Infecciosos/isolamento & purificação , Anti-Infecciosos/farmacocinética , Antifúngicos/isolamento & purificação , Antifúngicos/farmacologia , Antioxidantes/química , Antioxidantes/farmacologia , Proteínas de Transporte/genética , Proteínas de Transporte/isolamento & purificação , Proteínas de Transporte/farmacologia , Fusarium/efeitos dos fármacos , Fusarium/patogenicidade , Espécies Reativas de Oxigênio/metabolismo , Xanthomonas/efeitos dos fármacos , Xanthomonas/patogenicidade
4.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;45(11): 1002-1010, Nov. 2012. ilus
Artigo em Inglês | LILACS | ID: lil-650578

RESUMO

Ricinus communis L. is of great economic importance due to the oil extracted from its seeds. Castor oil has been used for pharmaceutical and industrial applications, as a lubricant or coating agent, as a component of plastic products, as a fungicide or in the synthesis of biodiesel fuels. After oil extraction, a castor cake with a large amount of protein is obtained. However, this by-product cannot be used as animal feed due to the presence of toxic (ricin) and allergenic (2S albumin) proteins. Here, we propose two processes for detoxification and allergen inactivation of the castor cake. In addition, we establish a biological test to detect ricin and validate these detoxification processes. In this test, Vero cells were treated with ricin, and cell death was assessed by cell counting and measurement of lactate dehydrogenase activity. The limit of detection of the Vero cell assay was 10 ng/mL using a concentration of 1.6 x 10(5) cells/well. Solid-state fermentation (SSF) and treatment with calcium compounds were used as cake detoxification processes. For SSF, Aspergillus niger was grown using a castor cake as a substrate, and this cake was analyzed after 24, 48, 72, and 96 h of SSF. Ricin was eliminated after 24 h of SSF treatment. The cake was treated with 4 or 8% Ca(OH)2 or CaO, and both the toxicity and the allergenic properties were entirely abolished. A by-product free of toxicity and allergens was obtained.


Assuntos
Animais , Alérgenos/efeitos dos fármacos , Aspergillus niger/crescimento & desenvolvimento , Compostos de Cálcio/farmacologia , Ricinus communis/efeitos dos fármacos , Inativação Metabólica , Alérgenos/toxicidade , Aspergillus niger/efeitos dos fármacos , Chlorocebus aethiops , Ricinus communis/toxicidade , Morte Celular/efeitos dos fármacos , Degranulação Celular/efeitos dos fármacos , Ativação Enzimática , Fermentação , L-Lactato Desidrogenase/metabolismo , Mastócitos/efeitos dos fármacos , Ricina/isolamento & purificação , Ricina/toxicidade , Fatores de Tempo , Testes de Toxicidade , /isolamento & purificação , /toxicidade , Células Vero
5.
Braz J Med Biol Res ; 45(11): 1002-10, 2012 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-22911344

RESUMO

Ricinus communis L. is of great economic importance due to the oil extracted from its seeds. Castor oil has been used for pharmaceutical and industrial applications, as a lubricant or coating agent, as a component of plastic products, as a fungicide or in the synthesis of biodiesel fuels. After oil extraction, a castor cake with a large amount of protein is obtained. However, this by-product cannot be used as animal feed due to the presence of toxic (ricin) and allergenic (2S albumin) proteins. Here, we propose two processes for detoxification and allergen inactivation of the castor cake. In addition, we establish a biological test to detect ricin and validate these detoxification processes. In this test, Vero cells were treated with ricin, and cell death was assessed by cell counting and measurement of lactate dehydrogenase activity. The limit of detection of the Vero cell assay was 10 ng/mL using a concentration of 1.6 x 10(5) cells/well. Solid-state fermentation (SSF) and treatment with calcium compounds were used as cake detoxification processes. For SSF, Aspergillus niger was grown using a castor cake as a substrate, and this cake was analyzed after 24, 48, 72, and 96 h of SSF. Ricin was eliminated after 24 h of SSF treatment. The cake was treated with 4 or 8% Ca(OH)2 or CaO, and both the toxicity and the allergenic properties were entirely abolished. A by-product free of toxicity and allergens was obtained.


Assuntos
Alérgenos/efeitos dos fármacos , Aspergillus niger/crescimento & desenvolvimento , Compostos de Cálcio/farmacologia , Inativação Metabólica , Ricinus communis/efeitos dos fármacos , Albuminas 2S de Plantas/isolamento & purificação , Albuminas 2S de Plantas/toxicidade , Alérgenos/toxicidade , Animais , Aspergillus niger/efeitos dos fármacos , Ricinus communis/toxicidade , Morte Celular/efeitos dos fármacos , Degranulação Celular/efeitos dos fármacos , Chlorocebus aethiops , Ativação Enzimática , Fermentação , L-Lactato Desidrogenase/metabolismo , Mastócitos/efeitos dos fármacos , Ricina/isolamento & purificação , Ricina/toxicidade , Fatores de Tempo , Testes de Toxicidade , Células Vero
6.
Peptides ; 29(4): 497-504, 2008 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-18262682

RESUMO

Ric c 1 and Ric c 3 are the major castor bean allergens. In order to identify continuous IgE-epitopes in Ric c 1 and Ric c 3, pools of sera from rats immunized with a pool of 2S albumin from these seeds, Ric c 1 and Ric c 3 overlapping synthetic peptides, were used to screen for IgE-binding epitopes. The allergenic properties were monitored by mast cell degranulation assays, histamine quantification and human-IgE binding. Large and small chains isolated from these proteins present allergenic properties. Four continuous epitopes were identified in Ric c 3 and two in Ric c 1. This knowledge may allow the induction of protective antibody responses to antagonize the IgE recognition.


Assuntos
Antígenos de Plantas/imunologia , Epitopos/imunologia , Imunoglobulina E/imunologia , Mastócitos/imunologia , Proteínas de Plantas/imunologia , Ricinus/imunologia , Albuminas 2S de Plantas , Alérgenos , Sequência de Aminoácidos , Animais , Antígenos de Plantas/isolamento & purificação , Antígenos de Plantas/metabolismo , Degranulação Celular , Mapeamento de Epitopos , Feminino , Humanos , Mastócitos/citologia , Dados de Sequência Molecular , Peptídeos/síntese química , Peptídeos/química , Proteínas de Plantas/isolamento & purificação , Proteínas de Plantas/metabolismo , Ratos , Ratos Endogâmicos , Alinhamento de Sequência
7.
Braz J Med Biol Res ; 39(11): 1435-44, 2006 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-17146556

RESUMO

Evidence based on immunological cross-reactivity and anti-diabetic properties has suggested the presence of insulin-like peptides in plants. The objective of the present study was to investigate the presence of insulin-like proteins in the leaves of Bauhinia variegata ("pata-de-vaca", "mororó"), a plant widely utilized in popular medicine as an anti-diabetic agent. We show that an insulin-like protein was present in the leaves of this plant. A chloroplast protein with a molecular mass similar to that of bovine insulin was extracted from 2-mm thick 15% SDS-PAGE gels and fractionated with a 2 x 24 cm Sephadex G-50 column. The activity of this insulin-like protein (0.48 mg/mL) on serum glucose levels of four-week-old Swiss albino (CF1) diabetic mice was similar to that of commercial swine insulin used as control. Further characterization of this molecule by reverse-phase hydrophobic HPLC chromatographic analysis as well as its antidiabetic activity on alloxan-induced mice showed that it has insulin-like properties. Immunolocalization of the insulin-like protein in the leaves of B. variegata was performed by transmission electron microscopy using a polyclonal anti-insulin human antibody. Localization in the leaf blades revealed that the insulin-like protein is present mainly in chloroplasts where it is also found associated with crystals which may be calcium oxalate. The presence of an insulin-like protein in chloroplasts may indicate its involvement in carbohydrate metabolism. This finding has strengthened our previous results and suggests that insulin-signaling pathways have been conserved through evolution.


Assuntos
Bauhinia/química , Cloroplastos/química , Diabetes Mellitus Experimental/tratamento farmacológico , Hipoglicemiantes/isolamento & purificação , Proteínas de Ligação a Fator de Crescimento Semelhante a Insulina/isolamento & purificação , Folhas de Planta/química , Animais , Autoanticorpos/sangue , Bauhinia/citologia , Bovinos , Cloroplastos/ultraestrutura , Cromatografia Líquida de Alta Pressão , Eletroforese em Gel de Poliacrilamida , Hipoglicemiantes/uso terapêutico , Imunoglobulina G/sangue , Proteínas de Ligação a Fator de Crescimento Semelhante a Insulina/uso terapêutico , Camundongos , Microscopia Eletrônica de Transmissão , Folhas de Planta/citologia
8.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;39(11): 1435-1444, Nov. 2006. ilus, graf
Artigo em Inglês | LILACS | ID: lil-437826

RESUMO

Evidence based on immunological cross-reactivity and anti-diabetic properties has suggested the presence of insulin-like peptides in plants. The objective of the present study was to investigate the presence of insulin-like proteins in the leaves of Bauhinia variegata ("pata-de-vaca", "mororó"), a plant widely utilized in popular medicine as an anti-diabetic agent. We show that an insulin-like protein was present in the leaves of this plant. A chloroplast protein with a molecular mass similar to that of bovine insulin was extracted from 2-mm thick 15 percent SDS-PAGE gels and fractionated with a 2 x 24 cm Sephadex G-50 column. The activity of this insulin-like protein (0.48 mg/mL) on serum glucose levels of four-week-old Swiss albino (CF1) diabetic mice was similar to that of commercial swine insulin used as control. Further characterization of this molecule by reverse-phase hydrophobic HPLC chromatographic analysis as well as its antidiabetic activity on alloxan-induced mice showed that it has insulin-like properties. Immunolocalization of the insulin-like protein in the leaves of B. variegata was performed by transmission electron microscopy using a polyclonal anti-insulin human antibody. Localization in the leaf blades revealed that the insulin-like protein is present mainly in chloroplasts where it is also found associated with crystals which may be calcium oxalate. The presence of an insulin-like protein in chloroplasts may indicate its involvement in carbohydrate metabolism. This finding has strengthened our previous results and suggests that insulin-signaling pathways have been conserved through evolution.


Assuntos
Animais , Bovinos , Camundongos , Bauhinia/química , Cloroplastos/química , Diabetes Mellitus Experimental/tratamento farmacológico , Hipoglicemiantes/isolamento & purificação , Proteínas de Ligação a Fator de Crescimento Semelhante a Insulina/isolamento & purificação , Folhas de Planta/química , Autoanticorpos/sangue , Bauhinia/citologia , Cromatografia Líquida de Alta Pressão , Cloroplastos/ultraestrutura , Eletroforese em Gel de Poliacrilamida , Hipoglicemiantes/uso terapêutico , Imunoglobulina G/sangue , Proteínas de Ligação a Fator de Crescimento Semelhante a Insulina/uso terapêutico , Microscopia Eletrônica de Transmissão , Folhas de Planta/citologia
9.
Biochimie ; 88(1): 59-68, 2006 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-16085351

RESUMO

We show here that serum of piaussu, a Neotropical characin fish, has the highest butyrylcholinesterase activity so far described for humans and fish. To clarify whether this cholinesterase could protect piaussu against anticholinesterase pesticides by scavenging organophosphates, we purified it 1700-fold, with a yield of 80%. Augmenting concentrations (from 0.01 to 20 mM) of butyrylthiocholine activated it. The pure enzyme was highly inhibited by chlorpyriphos-oxon (ki=10,434x10(6) M-1 min-1) and by the specific butyrylcholinesterase inhibitor, isoOMPA (ki=45.7x10(6) M-1 min-1). Electrophoresis of total serum and 2-D electrophoresis of the purified cholinesterase showed that some enzyme molecules could circulate in piaussu serum as heterogeneously glycosylated dimers. The enzyme's N-terminal sequence was similar to sequences found for butyrylcholinesterase from sera of other vertebrates. Altogether, our data present a novel butyrylcholinesterase with the potential of protecting a fish from poisoning by organophosphates.


Assuntos
Butirilcolinesterase/sangue , Peixes/sangue , Sequência de Aminoácidos , Animais , Butirilcolinesterase/isolamento & purificação , Butirilcolinesterase/metabolismo , Butiriltiocolina/metabolismo , Clorpirifos/análogos & derivados , Clorpirifos/farmacologia , Inibidores da Colinesterase/farmacologia , Eletroforese em Gel Bidimensional , Eletroforese em Gel de Poliacrilamida , Humanos , Dados de Sequência Molecular , Intoxicação por Organofosfatos , Paraoxon/análogos & derivados , Paraoxon/farmacologia , Intoxicação/prevenção & controle , Alinhamento de Sequência , Tetraisopropilpirofosfamida/farmacologia
10.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;36(9): 1167-1173, Sept. 2003. ilus, tab, graf
Artigo em Inglês | LILACS | ID: lil-342857

RESUMO

Since the discovery of bovine insulin in plants, much effort has been devoted to the characterization of these proteins and elucidation of their functions. We report here the isolation of a protein with similar molecular mass and same amino acid sequence to bovine insulin from developing fruits of cowpea (Vigna unguiculata) genotype Epace 10. Insulin was measured by ELISA using an anti-human insulin antibody and was detected both in empty pods and seed coats but not in the embryo. The highest concentrations (about 0.5 ng/æg of protein) of the protein were detected in seed coats at 16 and 18 days after pollination, and the values were 1.6 to 4.0 times higher than those found for isolated pods tested on any day. N-terminal amino acid sequencing of insulin was performed on the protein purified by C4-HPLC. The significance of the presence of insulin in these plant tissues is not fully understood but we speculate that it may be involved in the transport of carbohydrate to the fruit


Assuntos
Animais , Bovinos , Insulina , Proteínas de Plantas , Plantas , Homologia de Sequência de Aminoácidos , Western Blotting , Cromatografia Líquida de Alta Pressão , Eletroforese em Gel de Poliacrilamida , Ensaio de Imunoadsorção Enzimática , Insulina , Peso Molecular , Proteínas de Plantas , Plantas
11.
Braz J Med Biol Res ; 36(9): 1167-73, 2003 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-12937781

RESUMO

Since the discovery of bovine insulin in plants, much effort has been devoted to the characterization of these proteins and elucidation of their functions. We report here the isolation of a protein with similar molecular mass and same amino acid sequence to bovine insulin from developing fruits of cowpea (Vigna unguiculata) genotype Epace 10. Insulin was measured by ELISA using an anti-human insulin antibody and was detected both in empty pods and seed coats but not in the embryo. The highest concentrations (about 0.5 ng/micro g of protein) of the protein were detected in seed coats at 16 and 18 days after pollination, and the values were 1.6 to 4.0 times higher than those found for isolated pods tested on any day. N-terminal amino acid sequencing of insulin was performed on the protein purified by C4-HPLC. The significance of the presence of insulin in these plant tissues is not fully understood but we speculate that it may be involved in the transport of carbohydrate to the fruit.


Assuntos
Fabaceae/química , Insulina/análise , Proteínas de Plantas/análise , Homologia de Sequência de Aminoácidos , Animais , Western Blotting , Bovinos , Cromatografia Líquida de Alta Pressão , Eletroforese em Gel de Poliacrilamida , Ensaio de Imunoadsorção Enzimática , Fabaceae/genética , Insulina/genética , Peso Molecular , Proteínas de Plantas/genética
12.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;33(2): 191-8, Feb. 2000.
Artigo em Inglês | LILACS | ID: lil-252294

RESUMO

The presence of phaseolin (a vicilin-like 7S storage globulin) peptides in the seed coat of the legume Phaseolus lunatus L. (lima bean) was demonstrated by N-terminal amino acid sequencing. Utilizing an artificial seed system assay we showed that phaseolin, isolated from both cotyledon and testa tissues of P. lunatus, is detrimental to the nonhost bruchid Callosobruchus maculatus (F) (cowpea weevil) with ED50 of 1.7 and 3.5 percent, respectively. The level of phaseolin in the seed coat (16.7 percent) was found to be sufficient to deter larval development of this bruchid. The expression of a C. maculatus-detrimental protein in the testa of nonhost seeds suggests that the protein may have played a significant role in the evolutionary adaptation of bruchids to legume seeds


Assuntos
Animais , Besouros/fisiologia , Fabaceae/química , Proteínas de Plantas/isolamento & purificação , Sementes/química , Sequência de Aminoácidos , Doenças das Plantas/parasitologia , Proteínas de Plantas/análise
13.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;25(6): 567-82, 1992. ilus
Artigo em Inglês | LILACS | ID: lil-109071

RESUMO

A 1.9s albumin having allergenic activity and denoted Ric c III was isolated from an alcohol extract of defatted Ricinus communis seeds CB-1A, as a homogeneous protein by ion -exchange chromatography on SP-Sephadex, gel filtration on Sephadex G-75 and preparative polyacrylamide gel electrophoresis (6 mg Ric cIII/g CB-1A). The protein contained approximately 98 amino acid residues distributed in 2 chains of 67 anmd 34 residues, a molecular weight of 11.239 based on amino acid composition and pI=4.9 Ric c III can be aligned, on the basis of amino acid composition and partial amino acid sequence data, with residues 18 to 50 (51) and 66 to 130 of the 2S albumin precursor predicted by the cDNA data of S. D. Irwin, J. N. Ken, J. B. C. Findlary and J. M. Lord (Molecular and General Genetics, 222:400-408, 1990). The present data identify Ric c III as the second allergenic 2S storage albumin coded by this DNA


Assuntos
Albuminas , Alérgenos/farmacologia , Ricinus/isolamento & purificação , Proteínas de Vegetais Comestíveis
14.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;24(2): 141-3, 1991. tab
Artigo em Inglês | LILACS | ID: lil-99447

RESUMO

Antigen 5.1 was isolated from the most acidic fraction of castor bean allergens (CB-1A) by gel filtration on Sephadex G-75 followed by polyacrylamide gel electrophoresis (PAGE) (yield: 6.2 mg antigen 5.1/g CB-1A). This antigen was homogeneous by the criteria of PAGE, isoelectric focusing, SDS-PAGE, immunoelectrophoresis and gel filtration. The antigen has an apparent molecular mass of 12 ñ 2 kDa and an isoelectric point of pH 5.1. Antigen 5.1 lacks proline, phenylalanine, threonine and tryptophan. It was immunochemically identical to one of the three immunoprecipitation lines presented by CB-1A by the Ouchterlony technique, and was positive when tested (250 *g) by IgE-mediated passive cutaneous anaphylaxis in LOU.M rats


Assuntos
Antígenos/isolamento & purificação , Sementes , Ricinus communis/imunologia , Alérgenos/análise , Aminoácidos/análise , Cromatografia em Gel
15.
An. acad. bras. ciênc ; 62(1): 17-24, mar. 1990. tab
Artigo em Inglês | LILACS | ID: lil-92236

RESUMO

A glycoprotein, RC-13, isolated from Ricinus communis seeds was reduced, S-alkylated and cleaved by trypsin. The tryptic digest was fractionated by ion-exchange chromatography and a glycopeptide was isolated and purified by high-voltage paper electrophoresis. When submitted to amino acid and carbohydrate analyses this major glycopeptide showed the following chemical composition: Lys1, Asp1, Thr2, Ser4, Glu1, Pro2, Gly2, Ala2, Val2, GlcN6, Man6 and Gal8. Hydrazynolysis positioned Ser as the C-terminal residue. It is postulated that this glycopeptide belongs to the C-terminal region of the allergen


Assuntos
Alérgenos/isolamento & purificação , Aminoácidos/análise , Ricinus communis/análise , Glicopeptídeos/isolamento & purificação , Sementes/análise , Mapeamento de Peptídeos
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