Simultaneous electrophoretic analysis of proteins of very high and low molecular weights using low-percentage acrylamide gel and a gradient SDS-PAGE gel

2006 ◽  
Vol 27 (20) ◽  
pp. 3935-3938 ◽  
Author(s):  
Eduard Casas-Terradellas ◽  
Francesc R. Garcia-Gonzalo ◽  
Ouadah Hadjebi ◽  
Ramon Bartrons ◽  
Francesc Ventura ◽  
...  
Author(s):  
A. K. Mandal ◽  
R. K. Das ◽  
A. Maity ◽  
G. R. Sahoo

The present study was undertaken to isolate gastrin peptide from the antral tissue of broiler chicken. The chicken antrums, i.e. tissue pieces from a narrow zone at gizzard – duodenal junction were collected, boiled in distilled water, followed by centrifugation at 0° C. The supernatant was collected, added to isopropanol and stirred overnight. After addition of dichloromethane, the aqueous phase was partitioned, aspirated and lyophilized. The electrophoretic analysis (SDS-PAGE) of the antral sample was carried out after running it along with a reference protein marker. Characterization of the antral extract revealed a total of eleven peptide bands having relative molecular weights (Mr) ranging from 4.6 to114.5 kDa, out of which peptides having Mr of 22.6 and 26.3 kDa were major ones. The protein or peptide band showing the lowest relative molecular weight (Mr, 4.6 kDa) was identified as the gastrin.


2011 ◽  
Vol 60 (2) ◽  
pp. 149-154
Author(s):  
KAMELIA M. OSMAN ◽  
ZEINAB M. S. AMIN ◽  
MAGDY A.K. ALY ◽  
HANY HASSAN ◽  
WALEED S. SOLIMAN

Aeromonas microorganisms normally grow at temperatures between 5 degrees C and 45 degrees C and therefore should have high thermotolerance. Thus it was of interest to find out whether A. hydrophila, A. caviae and A. veronii biovar sobria serovars respond to abrupt temperature changes with a heat shock-like response. To this end the present study was undertaken to determine whether Aeromonas species exhibits a heat shock response to different temperatures and time factors. The response of Aeromonas serovars to 24 h and 48 h of thermal stress at 25 degrees C, 42 degrees C and 50 degrees C involved the synthesis of 12-18 heat shock proteins (HSPs) bands with molecular weights ranging between 83.5-103.9 kDa in the high HSP molecular mass and 14.5-12.0 as low molecular mass HSP. Electrophoretic analysis of the HSPs showed that the serovars do not cluster very tightly and also that they are distinct from each other.


2018 ◽  
Vol 10 (1) ◽  
pp. 41-46
Author(s):  
R.N. OLADOSU-AJAYI ◽  
I.T. OMONIYI ◽  
H.E. DIENYE

Oladosu-Ajayi RN, Omoniyi IT, Dienye HE. 2018. Muscle protein bands resolved by Sarotherodon melanotheron from fresh and brackish water habitats. Nusantara Bioscience 10: 40-45. An electrophoretic analysis of muscle protein of Sarotherodon melanotheron from freshwater (Eleiyele Reservoir, Ibadan, Nigeria) and brackish water (Lekki Lagoon, Lagos, Nigeria) was carried out using the Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). The protein banding patterns for the fish species were distinguishable. The freshwater S. melanotheron samples displayed 15-22 protein bands with the male samples having the highest while the brackish water S. melanotheron samples displayed 13-20 protein bands with the female having the highest. The freshwater S. melanotheron were also observed to have resolved a higher range of protein bands of molecular weights ranging between 20 kd to 99 kd than the brackish water species, which resolved protein bands of lower molecular weights ranging between 20 kd to 95 kd. The electrophoretic analysis of muscle proteins revealed that SDS-PAGE can be considered a good taxonomic criterion to differentiate among and within fish species.


2018 ◽  
Vol 30 (2) ◽  
pp. 19-28
Author(s):  
A. J. Oludare ◽  
J. I. Kioko ◽  
A. A. Akeem ◽  
A. T. Olumide ◽  
K. R. Justina ◽  
...  

Nine accessions of Bambara groundnut (Vigna subterranea (L.) Verdc.,syn. Voandzeia subterranea (L.) Thouars ex DC.)  obtained from National Centre for Genetic Resources and Biotechnology (NACGRAB), Ibadan, Oyo state, were assessed for their genetic and phylogenetic relatedness through electrophoretic analysis of the seed proteins. 0.2g of the seeds were weighed and macerated with mortar and pestle in 0.2M phosphate buffer containing 0.133M of acid (NaH2PO4) and 0.067 of base (Na2HPO4) at pH 6.5. Protein characterization with standard marker revealed that the seeds of the nine accessions contained proteins (B.S.A, Oval Albumin, Pepsinogen, Trypsinogen and Lysozyme) with molecular weights ranging from 66kda and above, 45 – 65 kDa, 44 – 33 kda, 32-24 kDa and 23-14 kDa, respectively. The student T-test revealed that accessions B, C, E, F, H and I have molecular weights not significantly different from one another (P<0.05) while samples A, D and G showed significantly different values (P>0.05). All the accessions had at least two proteins and two major bands in common. The study revealed intra-specific similarities and genetic diversity in protein contents among the nine accessions of Bambara groundnut (Vigna subterraranea (L.) Verdc.syn


Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1244
Author(s):  
Malik Adil Nawaz ◽  
Tanoj Kumar Singh ◽  
Regine Stockmann ◽  
Hema Jegasothy ◽  
Roman Buckow

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.


2013 ◽  
Vol 76 (17-18) ◽  
pp. 1163-1169
Author(s):  
Emanuel Marques da Silva ◽  
Teresa Maria Marques dos Santos ◽  
José Filipe Teixeira Ganança ◽  
Jan Jacek Slaski ◽  
Miguel Â. A. Pinheiro de Carvalho

1989 ◽  
Vol 9 (8) ◽  
pp. 3377-3384 ◽  
Author(s):  
J Papkoff

The int-1 proto-oncogene is a target for insertional activation of transcription by mouse mammary tumor virus in many murine mammary tumors. Whereas no expression of int-1 is seen in normal mammary tissue, int-1 RNA can be detected in normal mice in the neural tubes of midgestation embryos and in postmeiotic spermatocytes from adult testes. I report here the results of a study in which several different antibodies against synthetic peptides were produced and used to characterize the processing and secretion of int-1 protein. CHO cells were transfected with an inducible int-1 expression vector that was subsequently amplified to generate cell lines expressing very high levels of int-1 protein. Immunoprecipitation of [35S]cysteine-labeled cell lysates from these CHO cells yielded large amounts of four immature forms of int-1 glycoprotein (molecular weights of 36,000, 38,000, 40,000, and 42,000). A significant fraction of these int-1 species formed disulfide-linked multimers. Pulse-chase and glycosidase digestion studies demonstrated that some of the immature species of int-1 protein move through the secretory pathway and are processed to a mature heterogeneous glycoprotein with a molecular weight of about 44,000. Suramin treatment of the CHO cells during pulse-chase experiments increased the amount of 44,000-molecular-weight int-1 protein in the culture medium.


1995 ◽  
Vol 25 (2) ◽  
pp. 229-232
Author(s):  
Sergio Echeverrigaray

Morphological and proteic modifications in Nicotiana tabacum L. transformed by Agrobacterium rhizogenes were evaluated by the comparison of normal and transformant plants regenerated from hairy-roots formed by the strains A4 or IB-642 of A. rhizogenes. Changes in apical dominance were observed in IB-642 transformants, which exhibited an abnormal development of axiliary buds. The electrophoretic analysis indicated an increase in peroxidase activity and the induction of several isozymes of this complex in the transformants. The SDS-PAGE patterns comparison allows to identify several changes, specially, the increase in 31-33 and 54 kD polypeptides in the transformants.. Biochemical analysis suggests the induction of a pathogen or stress like response of the transformants due to the high auxin concentration codified by A. rhizogenes T-DNA incorporated to the plant genome.


2016 ◽  
Vol 12 ◽  
pp. 1372-1379 ◽  
Author(s):  
Stefan Mark ◽  
Hubert Wadepohl ◽  
Markus Enders

A series of Cr(III) complexes based on quinoline-cyclopentadienyl ligands with additional hemilabile side arms were prepared and used as single-site catalyst precursors for ethylene polymerization. The additional donor functions interact with the metal centers only after activation with the co-catalyst. Evidence for this comes from DFT-calculations and from the differing behavior of the complexes in ethylene polymerization. All complexes investigated show very high catalytic activity and the additional side arm minimizes chain-transfer reactions, leading to increase of molecular weights of the resulting polymers.


2000 ◽  
Vol 66 (1) ◽  
pp. 252-256 ◽  
Author(s):  
Katsuichi Saito ◽  
Kazuya Kondo ◽  
Ichiro Kojima ◽  
Atsushi Yokota ◽  
Fusao Tomita

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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