scholarly journals Bark storage Protein in Peach, Plum, and Cherry Trees

HortScience ◽  
1995 ◽  
Vol 30 (4) ◽  
pp. 756A-756
Author(s):  
M.P. Bañados ◽  
M.S. Santiago ◽  
C. Eterovic
Keyword(s):  
Amino Acids ◽  
Storage Proteins ◽  
Protein Pattern ◽  
Fruit Trees ◽  
Sds Page ◽  
Bark Storage Proteins ◽  
Specific Proteins ◽  
Main Protein ◽  
Bark Storage Protein ◽  
Cherry Trees

The main form of nitrogen reserves during overwintering are amino acids and proteins. Specific proteins called bark storage proteins (BSP) have been characterized in many tree species. To identify BSPs in `O'Henry' peach, `Angeleno' plum, and `Early Burlat' cherry trees, samples of bark were collected from January through December 1993 from trees growing under field conditions in Santiago, Chile. SDS-PAGE analyses were used to characterize the seasonal variation on the protein pattern on the bark of those Prunus species. A 60 kDa BSP was identified in the bark of all three species, which corresponds to the main protein present in the bark during the winter. This protein may play an important role as a nitrogen reserve in these fruit trees.

scholarly journals Free amino acids in the xylem sap of pear trees during dormancy

2016 ◽  
Vol 46 (7) ◽  
pp. 1136-1141 ◽  
Author(s):  
Anderson Carlos Marafon ◽  
Flavio Gilberto Herter ◽  
Fernando José Hawerroth ◽  
Adriana Neutzling Bierhals
Keyword(s):  
Amino Acids ◽  
Water Content ◽  
Free Amino Acids ◽  
Free Amino ◽  
Storage Proteins ◽  
Xylem Sap ◽  
Fruit Trees ◽  
Temperate Climate ◽  
Pear Trees ◽  
Effective Use

ABSTRACT: Storage and remobilization are considered key processes for the effective use of nitrogen in temperate fruit trees. As dormancy begins, storage proteins are synthesized, coinciding with a reduction in the levels of free amino acids. Consequently, as dormancy breaks, these storage proteins are degraded, and an increase in the concentrations of amino acids occurs, in order to support new growth. The objective of this study was to evaluate water content of different vegetative tissues (buds, bark, and bole wood), volume of xylem sap, and free amino acid concentrations of xylem sap, during winter dormancy of Hosui Japanese pear trees (VL). Plant material was obtained from the Embrapa Temperate Climate experimental orchard at Pelotas, in the state of Rio Grande do Sul, Brazil. Xylem sap was extracted from the branches with the aid of a vacuum pump, and the free amino acids were determined by gas chromatography, using the EZ kit: Faast GC/FID (Phenomenex). Water content of buds, as well as the volume of sap and concentrations of both aspartic acid and asparagine, substantially increased over time, reaching maximum values in the phase preceding sprouting.

scholarly journals COLD ACCLIMATION IN THE LEAVES OF SIBLING DECIDUOUS AND EVERGREEN PEACH: ALTERATIONS IN DEHYDRIN AND BARK STORAGE PROTEINS

HortScience ◽  
1995 ◽  
Vol 30 (2) ◽  
pp. 190f-191
Author(s):  
Rajeev Arora ◽  
Michael Wisniewski ◽  
Lisa J. Rowland
Keyword(s):  
Cold Acclimation ◽  
Cold Tolerance ◽  
Prunus Persica ◽  
Storage Proteins ◽  
Seasonal Pattern ◽  
Bark Tissue ◽  
Bark Storage Proteins ◽  
Source Sink ◽  
Favorable Conditions ◽  
Bark Storage Protein

Seasonal pattern of cold tolerance and proteins were studied in the leaves of sibling deciduous and evergreen peach (Prunus persica). In contrast to deciduous peach that undergoes endodormancy in fall, evergreen peach does not (leaves are retained and shoot tips elongate under favorable conditions) (Arora et al., Plant Physiol. 99:1562-1568). Cold tolerance (LT50) was assessed using electrolyte leakage method. Proteins were separated by SDS-PAGE. Electroblots were probed with anti-dehydrin (Dr. T. Close) and anti-19 kD, peach bark storage protein (BSP) antibodies. LT50 of leaves successively increased from about -7C (18 Aug.) to -15C and -11.5C (23 Oct.) in deciduous and evergreen genotypes, respectively. The most apparent change in the protein profiles was the accumulation of a 60-kD protein during cold acclimation in the leaves of deciduous trees; however, it did not change significantly in evergreen peach. Immunoblots indicate that 60-kD protein is a dehydrin protein. PAGE and immunoblots indicated that 19-kD BSP disappeared progressively during summer through fall in the leaves of deciduous peach, but accumulated to large amounts in bark tissues. Similar inverse relationship for its accumulation in leaf vs. bark tissue was not evident in evergreen peach. Results indicate that BSP expression may be regulated by altered source/sink relationship.

scholarly journals Lectins from Pisum arvense seeds behave differently from storage proteins during germination in the darkness

2000 ◽  
Vol 12 (3) ◽  
pp. 255-262 ◽  
Author(s):  
LUIZA IZABEL M. MOREIRA DA SILVA ◽  
MÁRCIO VIANA RAMOS ◽  
JOÃO BATISTA CAJAZEIRAS ◽  
PATRÍCIA RODRIGUES FERREIRA ◽  
CARLOS ALBERTO V. CARVALHO ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Proteolytic Enzymes ◽  
Seed Proteins ◽  
High Molecular Mass ◽  
Mass Storage ◽  
Pisum Arvense ◽  
Germination Process ◽  
Sds Page ◽  
Haemagglutinating Activity ◽  
Main Protein

ABSTRACT - The mobilization of seed proteins from Pisum arvense L. during germination in the absence of light was studied. The seeds were found to be completely consumed 22 days after germination and seedlings ceased growth after the 18th day. SDS-PAGE indicated that the main protein bands correspond to high molecular mass storage proteins which undergo proteolysis in the initial stages of germination and are not detected after the 7th day of germination. However, the corresponding lectin profiles were detected during the entire germination process, suggesting that these proteins are strongly resistant to seed proteolytic enzymes and should be important for seedling establishment. Furthermore, haemagglutinating activity in cotyledons was detected until 22 days after germination, indicating that the lectins remain active even in senescent cotyledons.

scholarly journals 147 A 27-kDa Rhododendron Deacclimation Protein is Related to ABA Stress Ripening/Water Deficit Stress Inducible Family of Proteins

HortScience ◽  
2000 ◽  
Vol 35 (3) ◽  
pp. 415A-415
Author(s):  
Rajeev Arora ◽  
Chon-Chong Lim
Keyword(s):  
Amino Acids ◽  
Water Deficit ◽  
Aromatic Amino Acids ◽  
Water Deficit Stress ◽  
Compositional Bias ◽  
Sds Page ◽  
The Family ◽  
Specific Proteins ◽  
Controlled Freezing

Many reports have shown the accumulation of specific proteins associated with cold acclimation in plants. However, there is a scarcity of data on the physiological and/or biochemical changes associated with deacclimation process. This study was initiated to determine protein changes specifically associated with deacclimation in Rhododendron. Current-year leaves were collected from three Rhododendron cultivars (`Chionoides', `Grumpy Yellow', and `Vulcanís Flame'; ≈4-year-old rooted cuttings) during natural non-acclimated (June), cold-acclimated (January), and deacclimated (May) state. Leaf freezing tolerance was evaluated using controlled freezing protocol (Lim et al. 1998, J. Amer. Soc. Hort. Sci. 123:246–252). Seasonal SDS-PAGE profiles exhibited a distinct accumulation of 27 kDa protein in deacclimated and nonacclimated tissues, but this protein was essentially undetectable in cold acclimated tissues of all three cultivars. Further characterization of this polypeptide, labeled as RhDAP27 (for rhododendron deacclimation protein), revealed that it has an iso-electric point of 6.5, has a compositional bias for Glu/Gln (13.9%), His (11.4%), Gly (11%), Ala (10%), Lys (8.3%), and Asp/Asn (8.1%)—hydrophilic amino acids constitutedabout 54% of the total amino acids while 40% were nonpolar, aliphatic amino acids (Gly, Ala, Val, Leu, Ile, Pro) and only 6% were aromatic amino acids (Phe and Tyr). Micro-sequencing of the four peptides produced by partial cleavage of RhDAP27 revealed a striking homology of RhDAP27 with two proteins (from Mesembryanthemum crystallinum and Pinus taeda) that belong to the family of ABA stress ripening/water deficit stress inducible proteins.

Prediction of root damaging during mechanical shaking of fruit trees

2014 ◽  
Vol 10 (1) ◽  
pp. 1-15
Author(s):  
Z. Láng
Keyword(s):  
Field Experiments ◽  
Calculated Data ◽  
Fruit Trees ◽  
List Type ◽  
Structure Model ◽  
Root Damage ◽  
Set Up ◽  
Simple Tree ◽  
The Given ◽  
Cherry Trees

The possible effect of shaker harvest on root damage of 10-year-old cherry trees was studied on a simple tree structure model. The model was composed of elastic trunk and rigid main roots, the ends of which were connected to the surrounding soil via springs and dumping elements. Equations were set up to be able to calculate the relation between shaking height on the trunk and strain in the roots. To get the data for root break and their elongation at different shaking heights on the trunk, laboratory and field experiments were carried out on cherry trees and on their roots. Having evaluated the measured and calculated data it could be concluded that root damage is to be expected even at 3.6% strain and the risk of it increases with increased trunk amplitudes, i.e.with the decrease of shaking heightat smaller stem diameters (i.e. in younger plantation), andif the unbalanced mass of the shaker machine is too large for the given tree size.

scholarly journals Impact of Extraction Method on the Detection of Quality Biomarkers in Normal vs. DFD Meat

Foods ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1097
Author(s):  
Laura González-Blanco ◽  
Yolanda Diñeiro ◽  
Andrea Díaz-Luis ◽  
Ana Coto-Montes ◽  
Mamen Oliván ◽  
...  
Keyword(s):  
Extraction Method ◽  
Protein Pattern ◽  
Stress Protein ◽  
Electrophoretic Pattern ◽  
Extraction Methods ◽  
Sds Page ◽  
Weight Protein ◽  
Triton X ◽  
Protein Extractability ◽  
Selection Of

The objective of this work was to demonstrate how the extraction method affects the reliability of biomarker detection and how this detection depends on the biomarker location within the cell compartment. Different extraction methods were used to study the sarcoplasmic and myofibrillar fractions of the Longissimus thoracis et lumborum muscle of young bulls of the Asturiana de los Valles breed in two quality grades, standard (Control) or dark, firm, and dry (DFD) meat. Protein extractability and the expression of some of the main meat quality biomarkers—oxidative status (lipoperoxidation (LPO) and catalase activity (CAT)), proteome (SDS-PAGE electrophoretic pattern), and cell stress protein (Hsp70)—were analyzed. In the sarcoplasmic fraction, buffers containing Triton X-100 showed significantly higher protein extractability, LPO, and higher intensity of high-molecular-weight protein bands, whereas the TES buffer was more sensitive to distinguishing differences in the protein pattern between the Control and DFD meat. In the myofibrillar fraction, samples extracted with the lysis buffer showed significantly higher protein extractability, whereas samples extracted with the non-denaturing buffer showed higher results for LPO, CAT, and Hsp70, and higher-intensity bands in the electrophoretic pattern. These findings highlight the need for the careful selection of the extraction method used to analyze the different biomarkers considering their cellular location to adapt the extractive process.

scholarly journals Heat and Pressure Treatments on Almond Protein Stability and Change in Immunoreactivity after Simulated Human Digestion

Nutrients ◽  
2018 ◽  
Vol 10 (11) ◽  
pp. 1679 ◽  
Author(s):  
Elisabetta De Angelis ◽  
Simona Bavaro ◽  
Graziana Forte ◽  
Rosa Pilolli ◽  
Linda Monaci
Keyword(s):  
Protein Stability ◽  
Total Protein ◽  
Protein Pattern ◽  
Protein Quantification ◽  
Protein Profiling ◽  
Enzyme Linked Immunosorbent Assay ◽  
Total Protein Content ◽  
Bioinformatic Tools ◽  
Sds Page ◽  
Allergenic Proteins

Almond is consumed worldwide and renowned as a valuable healthy food. Despite this, it is also a potent source of allergenic proteins that can trigger several mild to life-threatening immunoreactions. Food processing proved to alter biochemical characteristics of proteins, thus affecting the respective allergenicity. In this paper, we investigated the effect of autoclaving, preceded or not by a hydration step, on the biochemical and immunological properties of almond proteins. Any variation in the stability and immunoreactivity of almond proteins extracted from the treated materials were evaluated by total protein quantification, Enzyme Linked Immunosorbent Assay (ELISA), and protein profiling by electrophoresis-based separation (SDS-PAGE). The sole autoclaving applied was found to weakly affect almond protein stability, despite what was observed when hydration preceded autoclaving, which resulted in a loss of approximately 70% of total protein content compared to untreated samples, and a remarkable reduction of the final immunoreactivity. The final SDS-PAGE protein pattern recorded for hydrated and autoclaved almonds disclosed significant changes. In addition, the same samples were further submitted to human-simulated gastro-intestinal (GI) digestion to evaluate potential changes induced by these processing methods on allergen digestibility. Digestion products were identified by High Pressure Liquid Chromatography-High Resolution Tandem Mass Spectrometry (HPLC-HRMS/MS) analysis followed by software-based data mining, and complementary information was provided by analyzing the proteolytic fragments lower than 6 kDa in size. The autoclave-based treatment was found not to alter the allergen digestibility, whereas an increased susceptibility to proteolytic action of digestive enzymes was observed in almonds subjected to autoclaving of prehydrated almond kernels. Finally, the residual immunoreactivity of the GI-resistant peptides was in-silico investigated by bioinformatic tools. Results obtained confirm that by adopting both approaches, no epitopes associated with known allergens survived, thus demonstrating the potential effectiveness of these treatments to reduce almond allergenicity.

A simple SDS-PAGE protein pattern from pitcher secretions as a new tool to distinguish Nepenthes species (Nepenthaceae)

2013 ◽  
Vol 100 (12) ◽  
pp. 2478-2484 ◽  
Author(s):  
Flore Biteau ◽  
Estelle Nisse ◽  
Sissi Miguel ◽  
Paul Hannewald ◽  
Vincent Bazile ◽  
...  
Keyword(s):  
Protein Pattern ◽  
Sds Page

scholarly journals Nutritional quality evaluation of Whitemouth croaker (Micropogonias furnieri) protein isolate

2014 ◽  
Vol 44 (2) ◽  
pp. 134-143
Author(s):  
William Renzo Cortez-Vega ◽  
Irene Rodrigues Freitas ◽  
Sandriane Pizato ◽  
Carlos Prentice
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nutritional Quality ◽  
Troponin I ◽  
Essential Amino Acids ◽  
Protein Isolate ◽  
Content Type ◽  
Sds Page ◽  
Apparent Bioavailability

Purpose – The purpose of this study was to isolate Whitemouth croaker protein by alkaline solubilization process and evaluate their nutritional quality to evaluate the bioavailability of essential amino acids. Design/methodology/approach – The proximate composition, essential amino acid composition, in vitro digestibility, apparent bioavailability, chemical score of amino acids and SDS-PAGE were determined for the isolated croaker proteins. Findings – The isolated protein showed a high level of protein 92.21 percent and low amount of lipids 0.57 percent. The protein is rich in lysine and leucine, 108.73 and 96.75 mg/g protein, respectively. The protein isolate had high digestibility, 94.32 percent, which indicates proper utilization of this protein source, while the tryptophan had lower bioavailability (12.58 mg amino acid/mg protein). The high chemical scores were found for the amino acids lysine, methionine+cysteine (6.79 and 5.14). SDS-PAGE of proteins extracted showed appearance of the heavy chain of myosin (220 kDa), actin (50 kDa) and other fractions, with molecular weight between 20 and 50 kDa, such as troponin I, C and T. Originality/value – The products obtained from croaker muscle can be incorporated as a high value supplements in human diets. The isolated protein exhibited a high content of essential amino acids and digestibility, indicating that the protein has a high nutritional quality.

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