Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia gladiata seeds

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Effects of a lectin-like protein isolated from Acacia farnesiana seeds on phytopathogenic bacterial strains and root-knot nematode

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Germination and anaerobic metabolism of seeds of Tabebuia cassinoides (Lam.) DC subjected to flooding and anoxia

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Do Terrestrial Tank Bromeliads in Brazil Create Safe Sites for Palm Establishment or Act as Natural Traps for Its Dispersed Seeds ?

This study shows for the first time that terrestrial tank bromeliads from Brazilian restinga can act as natural traps for dispersed palm Euterpe edulis seeds. Such bromeliads, which are shade intolerant, gain benefits by limiting palm recruitment since they hinder canopy formation and, consequently, increase luminosity over its aggregates.

Predation of the Buffy-fronted Seedeater Sporophila frontalis (Aves: Emberizidae) on Merostachys neesii (Poaceae: Babusoideae) seeds during a masting event in the Atlantic forest

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Cryopreservation of Dendrobium hybrid seeds and protocorms as affected by phloroglucinol and Supercool X1000

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Purification of a PHA-Like chitin-binding protein from Acacia farnesiana seeds: A time-dependent oligomerization protein

A lectin-like protein from the seeds of Acacia farnesiana was isolated from the albumin fraction, characterized, and sequenced by tandem mass spectrometry. The albumin fraction was extracted with 0.5 M NaCl, and the lectin-like protein of A. farnesiana (AFAL) was purified by ion-exchange chromatography (Mono-Q) followed by chromatofocusing. AFAL agglutinated rabbit erythrocytes and did not agglutinate human ABO erythrocytes either native or treated with proteolytic enzymes. In sodium dodecyl sulfate gel electrophoresis under reducing and nonreducing conditions, AFAL separated into two bands with a subunit molecular mass of 35 and 50 kDa. The homogeneity of purified protein was confirmed by chromatofocusing with a pI=4.0+/-0.5. Molecular exclusion chromatography confirmed time-dependent oligomerization in AFAL, in accordance with mass spectrometry analysis, which confers an alteration in AFAL affinity for chitin. The protein sequence was obtained by a liquid chromatography quadrupole time-of-flight experiment and showed that AFAL has 68% and 63% sequence similarity with lectins of Phaseolus vulgaris and Dolichos biflorus, respectively.

Purification, Characterization, and Preliminary X-Ray Diffraction Analysis of a Lactose-Specific Lectin from Cymbosema roseum Seeds

The unique carbohydrate-binding property of lectins makes them invaluable tools in biomedical research. Here, we report the purification, partial primary structure, carbohydrate affinity characterization, crystallization, and preliminary X-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds (CRLII). Isolation and purification of CRLII was performed by a single step using a Sepharose-4B-lactose affinity chromatography column. The carbohydrate affinity characterization was carried using assays for hemagglutination activity and inhibition. CRLII showed hemagglutinating activity toward rabbit erythrocytes. O-glycoproteins from mucine mucopolysaccharides showed the most potent inhibition capacity at a minimum concentration of 1.2 A mu g mL(-1). Protein sequencing by mass spectrometry was obtained by the digestion of CRLII with trypsin, Glu-C, and AspN. CRLII partial protein sequence exhibits 46% similarity with the ConA-like alpha chain precursor. Suitable protein crystals were obtained with the hanging-drop vapor-diffusion method with 8% ethylene glycol, 0.1 M Tris-HCl pH 8.5, and 11% PEG 8,000. The monoclinic crystals belong to space group P2(1) with unit cell parameters a = 49.4, b = 89.6, and c = 100.8 A....

The action of the testa upon the germination of seeds of Cucumis anguria L.

In negatively photoblastic seeds of Cucumis anguria L. the scarification of micropyle overcame the inhibitory effect of white light , although far-red radiation inhibited the germination in both intact and scarified seeds. The moistened testa powder transmitted more far-red than red radiation. Thus the testa could act as a filter of radiation and maintain a high far-red/red ratio at the photosensitive site of the embryo, which must be localized near the micropyle. © 1988 Academia.

Electrical conductivity of soybean soaked seeds. I. Effect of genotype

During the period from October/92 to September/94 experiments were carried out at the Seed Laboratory, FCAV/UNESP, Jaboticabal, SP, Brazil, using soybean seeds of different genotypes in order to evaluate the effect of genotype on the electrical conductivity (bulk conductivity) of soaked seeds. Seed moisture content (105 ± 3°C, 24 h), standard germination (four 50-seed samples, paper towel, 30°C), and vigor-accelerated aging (42°C, 48 h) were first determined. Undamaged soybean seeds were soaked in deionized water (four 50-seed samples, 75 ml, 25°C, 24 h) and electrical conductivity (μmhos.cm+1.g+1) was measured. Significant differences in conductivity were observed among genotypes having the same pattern of germination and vigor. The results have showed that electrical conductivity can be significantly influenced by genotype.

Oxalate determination in urine using an immobilized enzyme on Sorghum vulgare seeds in a flow injection conductimetric system

A flow-injection (FI) method was developed for the determination of oxalate in urine. It was based on the use of oxalate oxidase (E.C. 1.2.3.4) immobilized on ground seeds of the BR-303 Sorghum vulgare variety. A reactor was filled with this activated material, and the samples (200 μL) containing oxalate were passed through it, carried by a deionized water flow. The carbon dioxide produced by the enzyme reaction permeated through a microporous PTFE membrane, and was received in a water acceptor stream, promoting conductivity changes proportional to the oxalate concentration in the sample. The results obtained showed a useful linear range from 0.05 to 0.50 mmol dm-3. The proposed method, when compared with the Sigma enzymatic procedure, showed good correlation (Y = 0.006(±0.016) + 0.98(±0.019)X; r = 0.9995, Y = conductivity in μS, and X = concentration in mmol dm-3), selectivity, and sensitivity. The new immobilization approach promotes greater stability, allowing oxalate determination for 6 months. About 13 determinations can be performed per hour. The precision of the proposed method is about ± 3.2 % (r.s.d).

Germinative pretreatments to dormancy break in Guazuma ulmifolia Lam. seeds

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Evaluation of naturally and artificially aged seeds of Phaseolus vulgaris L.

Seed ageing is natural phenomenon that occurs in all seeds, including those stored in dry and low temperature rooms. Phaseolus vulgaris L. cv. 'Carioca' seeds harvested in five different years were stored in at 15°C. Seed samples were germinated and evaluated according to The Brazilian Rules for Testing Seeds. The newest seed sample was submitted to artificial ageing. Small (∼1g) samples of all materials (naturally and artificially aged) were ground and proteins extracted. Equal quantities of protein were loaded onto the gels and electrophoresis carried out. Although seeds submitted to 24, 48, 72 and 96 hours of artificial ageing did not show any statistical difference (5%) in relation to unaged seeds in physiological parameters related to emergence, some statistically different parameters related to dry matter and length of shoots and roots occurred. A 24 h of artificial ageing at 41°C improved these factors. Protein patterns were changed after 72 h of artificial ageing and naturally aged seeds showed alterations after two years storage at 15°C. Aged seeds, naturally and artificially, had decreasing germination, vigour, and changes in the characteristic banding pattern of proteins. Physiological parameters and electrophoresis examination showed that for naturally aged seeds physiological parameters were more sensitive while artificially aged seeds, (41°C/100% RH), had electrophoretic profiles that were more efficient for seed lot discrimination.