scholarly journals External morphological stages and protein variations along with the embryonic development of the longarm river prawn Macrobrachium tenellum (Smith, 1871)

2021 ◽  
Vol 49 (2) ◽  
pp. 202-211
Author(s):  
Marcelo U. García-Guerrero ◽  
Dulce M. Mateos-Guerrero ◽  
Juan J. Alpuche-Osorno ◽  
Rodolfo B. De los Santos-Romero
Keyword(s):  
Embryonic Development ◽  
Protein Concentration ◽  
Egg Size ◽  
Morphological Changes ◽  
Larval Rearing ◽  
Polyacrylamide Gels ◽  
Protein Extract ◽  
Molecular Weights ◽  
Sds Page ◽  
Page Electrophoresis

A good understanding of a given species' embryology is important to settle the larval rearing bases when juveniles are required for culture purposes or conservation programs. Changes in embryonic morphology, protein concentration, and protein type occurring in prawn eggs were analyzed in the present work. Berried females of Macrobrachium tenellum were collected in the Colotepec River, Oaxaca, Mexico. The eggs were taken from the ovigerous mass and embryonic stages classified by their color. Morphological changes in the embryos allowed identifying six embryonic stages based on color, egg size, and morphological features. Determinations of the protein extract were executed in SDS-PAGE (electrophoresis in polyacrylamide gels) and, subsequently, proteomic analyses were also performed. Protein bands along embryonic development and their molecular weights are presented and commented.

scholarly journals Quality Attributes of Ultra-High Temperature-Treated Model Beverages Prepared with Faba Bean Protein Concentrates

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1244
Author(s):  
Malik Adil Nawaz ◽  
Tanoj Kumar Singh ◽  
Regine Stockmann ◽  
Hema Jegasothy ◽  
Roman Buckow
Keyword(s):  
Physicochemical Properties ◽  
Faba Bean ◽  
Protein Concentration ◽  
High Concentration ◽  
Molecular Weights ◽  
Oil In Water ◽  
Sds Page ◽  
Lower Protein ◽  
7S Globulin ◽  
Bean Protein

The objective of this research was to develop a model faba bean drink with a high concentration of protein (>4% w/w). The protein molecular weights and frequency for both faba and soy were assessed using SDS-PAGE. Results showed similarities in the protein molecular weight of both faba and soy (mainly 11S globulin ~Glycinin and 7S globulin ~β-conglycinin). Thus, faba can be considered as a potential soy replica in plant-based milk beverages. Oil-in-water emulsions (5–8% w/w available protein) were prepared using faba bean protein concentrate (FPC), 1% sunflower oil, and 0.2% sunflower lecithin. These emulsions were used as model beverages and were further investigated for UHT processibility, stability, and physicochemical properties. The physicochemical properties of emulsions at various processing stages viz., coarse emulsification, homogenisation, and UHT, were measured. An increase in the protein concentration and thermal treatment resulted in an increased oil droplet size, coalescence and flocculation, and protein aggregation. Lower protein concentrations viz., 5–6%, showed greater negative ζ-potential, and thereby, high dispersibility through enhanced electrostatic repulsions than those of higher concentrations (7–8%). Furthermore, an increase in protein concentration and UHT treatment resulted in an increased creaming index. In total, 21 different volatile compounds were detected and quantified, representing different chemical classes, namely alcohols, aldehydes, ketones, esters, furan, and acids. These volatiles have major consequences for the overall flavour chemistry of the model beverage product. Overall, this study showed the potential for application of faba bean as a protein source in UHT-treated legume-based beverages and identified areas for further development.

scholarly journals Characterization of Gelatin Profile of Chicken Broiler (Gallus domestica) Bone Using SDS-PAGE Electrophoresis

ALCHEMY ◽  
2019 ◽  
Vol 7 (1) ◽  
pp. 7 ◽  
Author(s):  
Dewi Yuliani ◽  
Dhienda Risa Awalsasi ◽  
Akyunul Jannah
Keyword(s):  
Ammonium Sulfate ◽  
Protein Concentration ◽  
Peptide Fragments ◽  
Strong Base ◽  
Chicken Bone ◽  
Sds Page ◽  
Hydrolysis Of ◽  
Β Chain ◽  
Page Electrophoresis

<p>Gelatin, a proteinaceous additive, is obtained from hydrolysis of collagen in the bone, hide and skin of animals. As natural product, gelatin has been applied in many industries with various functions. This study attempt to characterize gelatin profile of broiler chicken (<em>Gallus domestica</em>) using SDS-PAGE electrophoresis. The chicken bone was pretreated using a strong base, sodium hydroxide, producing type B gelatin. The gelatin was purified through precipitation using the variation of ammonium sulfate concentrations (40-70%) and dialysis using cellophane membrane. The purified gelatin was characterized through SDS-PAGE electrophoresis. Based on electrophoresis visualization, reduction of band intensity by ammonium sulfate 40% showed removal of small peptide fragments. The remained gelatin showed two major bands, α-chains and a β-chain with the respective molecular weight of ~135 and ~245 kDa. The protein content of the unpurified gelatin (E1) was 71.65±0.60 mg/L.  The purified E1 gelatins by 40-70% of ammonium sulfate addition contained 61.42±3.90, 60.45±1.36, 59.89±0.24, and 55.32±1.05 mg/L of protein concentration, respectively.</p><p> </p><p>Keywords: chicken bone, gelatin profile, protein electrophoresis</p>

Affinity Chromatography of Human Factor VIII Using Human and Rabbit Antibodies to Factor VIII

1979 ◽  
Vol 42 (04) ◽  
pp. 1306-1315 ◽  
Author(s):  
Janet L Lane ◽  
H Ekert ◽  
A Vafiadis
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
Affinity Chromatography ◽  
Protein Concentration ◽  
Gel Filtration ◽  
Subunit Structure ◽  
Molecular Weights ◽  
Human Factor Viii ◽  
Sds Page ◽  
Normal Human

SummaryFactor VIII, purified by gel filtration on Sepharose 2B, has an 8 band multiple subunit structure, with molecular weights ranging from 30,000 to 230,000, on reduction and SDS-PAGE at a protein concentration of 400 μg/gel. Affinity chromatography of this factor VIII preparation with insolubilized haemophilic antibody to factor VIII showed that 45-81% VIII:C and 0-33% VIILRag were attached to the column. Elution of the column with 0.25 M CaCl2 did not show VIII:C or VIILRag in the eluate. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the dissociated protein, showed that 95 % of the protein bound by haemophilic antibody had a molecular weight similar to the low molecular weight subunits of the reduced factor VIII.In control experiments with normal Human IgG, 3% of VIII:C and 5% of VIILRag were attached to the column. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the protein, showed 2 faint bands with molecular weight consistent with heavy and light chains of IgG.Similar experiments with antibody to factor VIII showed that 67-83% of VIILC and 61-76% of VIII:Rag were attached to the column. Elution of the column with 0.25 M CaCl2 showed 10% of the applied VIII:C, but no VIII:Rag in the eluate. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the dissociated protein, showed an 8 band subunit structure similar to the reduced factor VIII.

scholarly journals Comparison of pectolytic and proteolytic activities of six clarifying commercial preparations. Incidence of secondary enzymatic activities on proteins in Champagne musts

OENO One ◽  
1996 ◽  
Vol 30 (2) ◽  
pp. 103
Author(s):  
Laurent Berthier ◽  
Richard Marchal ◽  
Alain Maujean
Keyword(s):  
Isoelectric Focusing ◽  
Total Protein ◽  
Protein Concentration ◽  
Enzymatic Activities ◽  
Pinot Noir ◽  
Molecular Weights ◽  
Sds Page ◽  
Isoelectric Points ◽  
Proteolytic Activities ◽  
Grape Varieties

<p style="text-align: justify;">In order ta estimate c1arifying aptitude and the effects of prefermentation treatment by commercial pectinases, polygalacturonase (PG), pectin Iyase (PL), pectinmethylesterase (PME) and proteolytic activities of six pectinases samples were studied. PG activity is preponderate and proportional to the relative protein concentration.</p><p style="text-align: justify;">These one, submitted to both SDS-PAGE and isoelectric focusing technics, show molecular weights ranging from 20 ta 100 kDa and isoelectric points ranging from 3.00 ta 7.40. Total protein of Champagne grape varieties Chardonnay (CH) and Pinot noir (PN) - were submitted to an isoelectric focusing. All of the pI's ranging from 3.30 to 4.55 (CH) and from 3.30 to 4.90 (PN). Proteases are put in evidence in commercial pectinases using fluorescamine- casein as substrate. However, they seem to have no incidence upon must proteins.</p>

Changes in casein composition of goats' milk during the course of lactation: physiological inferences and technological implications

1995 ◽  
Vol 62 (3) ◽  
pp. 431-439 ◽  
Author(s):  
Joanna R. Brown ◽  
Andrew J. R. Law ◽  
Christopher H. Knight
Keyword(s):  
Cation Exchange ◽  
Protein Concentration ◽  
Stage Of Lactation ◽  
Sds Page ◽  
Lower Protein ◽  
Kjeldahl Method ◽  
Compositional Changes ◽  
The Individual ◽  
Cheese Production ◽  
Peak Lactation

SummaryFive British Saanen goats were milk sampled during the first 39 weeks of lactation to determine changes in casein composition. Caseins were separated by anion- and cation-exchange FPLC to determine the relative amounts of the individual caseins. Acid, alkaline and SDS-PAGE were used to determine possible genetic polymorphisms and observe any lactational changes. Total casein nitrogen was determined using a micro-Kjeldahl method and this allowed the concentrations of individual caseins to be calculated. The milk of one animal, which had the deduced genotype αs1-CnAB, showed higher concentrations of both total and αs1-casein. The remainder of the group were either heterozygous αs1-CnBE or, more probably, homozygous αs1-CnE and produced milk of a generally lower protein concentration. Both FPLC and PAGE results showed that the relative amounts and concentrations of αs2-casein decreased with stage of lactation, consistent with its susceptibility to proteolysis. The relative amounts of the breakdown products of plasmin attack on β-casein, γ-caseins, were highly negatively correlated with milk yield (r = –0·942, P < 0·001) in the declining phase of lactation, reflecting the gradual involution of the gland at this time. The relative amount of κ-casein increased by ∼ 50% after peak lactation and its concentration almost doubled near the end of lactation. These compositional changes may alter the processing qualities of goats' milk in relation to cheese production.

Purification and characterization of tuberculin-active components from BCG

1975 ◽  
Vol 21 (12) ◽  
pp. 2019-2027
Author(s):  
M. Laguerre ◽  
R. Turcotte
Keyword(s):  
Physicochemical Properties ◽  
Guinea Pigs ◽  
Gel Filtration ◽  
Biologically Active ◽  
Polyacrylamide Gels ◽  
Active Components ◽  
Purification And Characterization ◽  
Molecular Weights ◽  
Antigenic Activity

The tuberculin activity of protoplasmic extracts isolated from living BCG was purified successively by gel filtration on Sephadex G-100 and G-75, and by electrophoresis on 7.5% and on gradient (6–18%) polyacrylamide gels. The tuberculin-active fractions, as determined in BCG-sensitized guinea pigs, were used as the starting material for each of the following fractionation steps.The physicochemical properties and the antigenic activity of the biologically active fractions have shown that a single component, or only a few ones with similar properties, possessed high tuberculin activity. These active components were proteins having relatively high molecular weights (about 72 000) and could behave as antigens.

scholarly journals Establishment of peritoneal liquid electrophoretogram from healthy horses and horses submitted to experimentally induced intestinal obstruction

2014 ◽  
Vol 66 (3) ◽  
pp. 665-671 ◽  
Author(s):  
A.F.S. Nogueira ◽  
P.A. Di Filippo ◽  
L.A. Anai ◽  
M.C. Vieira ◽  
K.M.M.G. Simplício ◽  
...  
Keyword(s):  
Intestinal Obstruction ◽  
Acute Phase ◽  
Acute Phase Proteins ◽  
Immunoglobulin A ◽  
Control Group ◽  
Protein Levels ◽  
Sds Page ◽  
Significant Difference ◽  
Page Electrophoresis ◽  
Experimentally Induced

The initial inflammatory stages of the colic syndrome include changes known as acute phase response. The aim of this study was to contribute with the establishment of reference values concerning the electrophoretogram of peritoneal liquid from healthy horses and horses submitted to experimentally induced intestinal obstruction. Twenty-one horses were allotted in four groups: duodenal obstruction (DG), ileum obstruction (IG), left-dorsal colon obstruction (MG), and control group (CG). Peritoneal liquid was sampled before obtruction (T0), with 3 hours of obstruction (T3) and 6, 30, 102 and 174 hours after desobstructing (T6, T30, T102 and T174, respectively). Total protein levels were determined by the biuret method and protein fractions were obtained by SDS-PAGE electrophoresis. The acute phase proteins (APP) identified were Immunoglobulin-A, ceruloplasmin, transferrin, albumin, α1-antitrypsin, heavy and light chains of immunoglobulin-G, haptoglobin, α1-acid glycoprotein and a still unnamed protein, which was called P24. There was no difference (P>0.3) in protein levels among groups, although a significant difference (P>0.05) was observed between distinct experimental moments in each group evidencing a higher response of the APP in the obstructed groups. The APP fractioning of the peritoneal liquid was standardized to establish a standard curve for healthy equines and those submitted to induced intestinal obstruction. Moreover, it was verified that the SDS-PAGE electrophoresis was sensitive and effective to help diagnose abdominal inflammatory processes.

scholarly journals Purification and Characterization of 2,6-β-d-Fructan 6-Levanbiohydrolase fromStreptomyces exfoliatus F3-2

2000 ◽  
Vol 66 (1) ◽  
pp. 252-256 ◽  
Author(s):  
Katsuichi Saito ◽  
Kazuya Kondo ◽  
Ichiro Kojima ◽  
Atsushi Yokota ◽  
Fusao Tomita
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Extracellular Enzyme ◽  
Molecular Weights ◽  
Sds Page ◽  
Monomeric Structure ◽  
Ph Range ◽  
Hydrolysis Of

ABSTRACT Streptomyces exfoliatus F3-2 produced an extracellular enzyme that converted levan, a β-2,6-linked fructan, into levanbiose. The enzyme was purified 50-fold from culture supernatant to give a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weights of this enzyme were 54,000 by SDS-PAGE and 60,000 by gel filtration, suggesting the monomeric structure of the enzyme. The isoelectric point of the enzyme was determined to be 4.7. The optimal pH and temperature of the enzyme for levan degradation were pH 5.5 and 60°C, respectively. The enzyme was stable in the pH range 3.5 to 8.0 and also up to 50°C. The enzyme gave levanbiose as a major degradation product from levan in an exo-acting manner. It was also found that this enzyme catalyzed hydrolysis of such fructooligosaccharides as 1-kestose, nystose, and 1-fructosylnystose by liberating fructose. Thus, this enzyme appeared to hydrolyze not only β-2,6-linkage of levan, but also β-2,1-linkage of fructooligosaccharides. From these data, the enzyme from S. exfoliatus F3-2 was identified as a novel 2,6-β-d-fructan 6-levanbiohydrolase (EC 3.2.1.64 ).

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