Gastrin peptide isolation in broiler chicken

2015 ◽  
Author(s):  
A. K. Mandal ◽  
R. K. Das ◽  
A. Maity ◽  
G. R. Sahoo
Keyword(s):  
Molecular Weight ◽  
Broiler Chicken ◽  
Electrophoretic Analysis ◽  
Distilled Water ◽  
Protein Marker ◽  
Molecular Weights ◽  
Sds Page ◽  
Reference Protein ◽  
Relative Molecular Weight

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.

scholarly journals Production and Characterization of Crude Protease from RS1 Isolate from silage of Floating Bladderwort (Utricularia gibba)

2020 ◽  
Vol 10 (3) ◽  
pp. 289-293
Author(s):  
Ace Baehaki ◽  
Arif Hidayat ◽  
Nuni Gofar ◽  
Rodiana Nopianti
Keyword(s):  
Molecular Weight ◽  
Production Time ◽  
Molecular Weights ◽  
Sds Page ◽  
Optimum Ph ◽  
Utricularia Gibba ◽  
Optimum Production ◽  
Optimum Ph And Temperature

The purpose of this research was to produce and characterizing crude protease from RS1 isolate of swamp plant silage. The optimum production time of RS1 isolate was 40 h. The optimum pH and temperature of protease from RS1 isolate were 10 and 45℃, respectively.  Ion Mg3+ increased RS1 protease whereas ion of Na+, K+, Fe2+, and Zn2+ inhibited protease from RS1 isolate. Study on the effect of metals ion indicated that protease from RS1 isolate was metaloenzyme. Based analysis on SDS-PAGE, the molecular weight of RS1 protease had 12 bands with molecular weights ranging from 34.75 kDa to 263.53 kDa.

CHARACTERIZATION OF COLLAGEN EXTRACT FROM THE SKINS OF COMMERCIAL FRESHWATER FISH

2015 ◽  
Vol 77 (33) ◽  
Author(s):  
Anida Aminudin ◽  
Shamsul Muhammad ◽  
Ruhil Hayati Hamdan ◽  
Rumaizi Shaari ◽  
Mariam Firdhaus Mad Nordin ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Freshwater Fish ◽  
Functional Property ◽  
Oreochromis Niloticus ◽  
Clarias Gariepinus ◽  
Cosmetic Products ◽  
Commercial Fish ◽  
Molecular Weights ◽  
Sds Page

Collagen was documented as a difficult and expensive protein to quantify due to its insoluble. It is particularly since solubility is a key functional property in a variety of applications such as healthcare and cosmetic products. The main aim of this study was to extract the collagens from the skins of commercial freshwater fish such as red tilapia (Oreochromis niloticus), catfish (Clarias gariepinus) and pangasius (Pangasius pangasius) together with characteristics defined for each type of collagen extraction. The extracted collagens were determined in their molecular weights by using SDS-PAGE and the structure of it was observed under SEM. The obtained molecular weight of all three commercial fish collagens is approximately >80kDa. The characteristics of each type of collagen were then defined by using appropriate analysis through this research.

CHARACTERIZATION OF HYDROPSYCHE SLOSSONAE (TRICHOPTERA: HYDROPSYCHIDAE) CAPTURE NET POLYPEPTIDES

2000 ◽  
Vol 132 (1) ◽  
pp. 59-68 ◽  
Author(s):  
L. Tessier ◽  
J.L. Boisvert ◽  
L.B-M. Vought ◽  
J.O. Lacoursière
Keyword(s):  
Molecular Weight ◽  
Sequence Data ◽  
Polyacrylamide Gel Electrophoresis ◽  
Current Trend ◽  
Cross Reactivity ◽  
Published Data ◽  
Molecular Weights ◽  
Sds Page ◽  
Terrestrial Insects

AbstractThe aim of this study was to characterize polypeptide components of the capture net spun by trichopteran larvae Hydropsyche slossonae (Banks) (Trichoptera: Hydropsychidae). Thirty-one polypeptide bands were identified by SDS – polyacrylamide gel electrophoresis (SDS–PAGE) from extracted net material, with molecular weights ranging from 8500 to 179 000. Comparison with published data on Bombyx mori (L.) (Lepidoptera: Bombycidae) silk, treated under similar denaturing conditions, shows that six low molecular weight polypeptides ranging between 8500 and 18 800 in the silk of H. slossonae are absent from that of B. mori; furthermore, two high molecular weight polypeptides (210 000 and 220 000) detected in the silk of B. mori are not present in that of H. slossonae. Differences between both groups are probably related to their mode of living and to the specific use of silk (in air versus under water). Our findings are consistent with the current trend in the literature that silk spun by aquatic and terrestrial insects, as well as those spun by different species, is apparently made of different biopolymers according to the protein constituents. Hence, the polypeptide characterization of silk, combined with sequence data and (or) antibodies cross-reactivity data, could represent a potential tool for taxonomic classification improvement of aquatic insects. These results could eventually be used to characterize hydropsychid capture net anomalies induced by environmental pollution.

scholarly journals α-Crystallin. The isolation and characterization of distinct macromolecular fractions

1971 ◽  
Vol 124 (2) ◽  
pp. 337-343 ◽  
Author(s):  
Abraham Spector ◽  
Lu-Ku Li ◽  
Robert C. Augusteyn ◽  
Arthur Schneider ◽  
Thomas Freund
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Chemical Difference ◽  
Molecular Weights ◽  
Isolation And Characterization ◽  
Different Populations ◽  
Molecular Weight Fractions

α-Crystallin was isolated from calf lens periphery by chromatography on DEAE-cellulose and gel filtration. Three distinct populations of macromolecules have been isolated with molecular weights in the ranges approx. 6×105−9×105, 0.9×106−4×106and greater than 10×106. The concentration of macromolecules at the molecular-weight limits of a population are very low. The members of the different populations do not appear to be in equilibrium with each other. Further, in those molecular-weight fractions investigated, no equilibrium between members of the same population was observed. The population of lowest molecular weight comprises 65–75% of the total material. The amino acid and subunit composition of the different-sized fractions appear very similar, if not identical. The only chemical difference observed between the fractions is the presence of significant amounts of sugar in the higher-molecular-weight fractions. Subunit molecular weights of approx. 19.5×103and 22.5×103were observed for all α-crystallin fractions.

scholarly journals Immunohistochemical and immunochemical characterization of a new endothelial cell-specific antigen.

1986 ◽  
Vol 34 (2) ◽  
pp. 209-214 ◽  
Author(s):  
J U Alles ◽  
K Bosslet
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Endothelial Cells ◽  
Endothelial Cell ◽  
Specific Antigen ◽  
Similar Molecular Weight ◽  
Immunochemical Characterization ◽  
Sds Page

A new monoclonal antibody (moab BW 200) of IgG3 kappa-isotype was generated which recognizes an epitope located on an antigen molecule restricted to human neoplastic and non-neoplastic endothelial cells. The molecular weight of the antigen was determined using immunoprecipitation analysis followed by SDS-PAGE. Despite its similar molecular weight to FVIII-RAG, the antigen detected by moab BW 200 was shown to be different from FVIII-RAG.

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 ).

Isolation and biochemical characterization of septate junctions: differences between the proteins in smooth and pleated varieties

1989 ◽  
Vol 93 (1) ◽  
pp. 123-131
Author(s):  
NANCY J. LANE ◽  
STEPHEN M. DILWORTH
Keyword(s):  
Periplaneta Americana ◽  
Biochemical Characterization ◽  
Septate Junction ◽  
Septate Junctions ◽  
Molecular Weights ◽  
Thin Sectioning ◽  
Sds Page ◽  
High Concentrations ◽  
Membrane Components

Septate junctions are found only in invertebrate tissues, and are almost ubiquitous within them. In arthropods, the two major types are the ‘pleated’ and the ‘smooth’ varieties. Using tissues from different species, including the cockroach Periplaneta americana, procedures have been established for obtaining membrane fractions selectively enriched in septate junctions. The junctions have been identified in pellets of these fractions by both thin sectioning and freeze-fracturing. SDS-PAGE of these membrane fractions reveals two major polypeptide species with apparent molecular weights of 22000–24000 and 17000–18000. Consistent differences in these apparent molecular weights are observed between the pleated and smooth varieties of septate junction. These polypeptides are probably integral membrane components, as they remain associated after treatment with high concentrations of urea. Evidence suggests a plane of weakness in the mid-line of the extracellular septal ribbons.

A PLASMINOGEN ACTIVATOR INHIBITOR (PAI-2) CIRCULATES IN TWO HIGH MOLECULAR WEIGHT FORMS IN PREGNANCY

1987 ◽  
Author(s):  
N A Booth ◽  
A Reith ◽  
B Bennett
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Plasminogen Activator ◽  
Apparent Molecular Weight ◽  
Late Pregnancy ◽  
Plasminogen Activator Inhibitor ◽  
Molecular Weights ◽  
Histiocytic Cell ◽  
Sds Page ◽  
Pai 1

Normal vascular endothelium and platelet α-granules contain an inhibitor of plasminogen activator (PAI-1) of about 48000 molecular weight, which is released by stimuli such as thrombin. An immunologically distinct inhibitor (PAI-2) of about 47000 molecular weight has been purified from placenta and from a histiocytic cell line U-937. The level of PA-inhibition in plasma is raised in late pregnancy and this may be due to increases in PAI-1 or in PAI-2 or in both.Using SDS-PAGE and zymography on fibrin/plasminogen /u-PA detector gels, we have found that normal plasma contains a band of inhibition of apparent molecular weight 40000, which can be neutralised by antiserum raised against PAI-1. Pregnancy plasma contained this band as well as additional inhibitor bands of apparent molecular weights 75000 and 130000. The novel high molecular weight PA-inhibitors were detectable by zymography at about 12 weeks gestation. They were specific for plasminogen activator and did not inhibit plasmin. They were inhibited by antiserum raised against PAI-2 from U-937 cells (a gift from Dr EKO Kruithof) and thus are immunologically related to PAI-2. They may represent circulating complexes of PAI-2 with another protein or aggregates of PAI-2, which retain inhibitory activity after SDS-PAGE. PAI-2 appears to represent a pregnancy associated protein that circulates in a number of different molecular weight forms.

Characterization Of The ADP-Induced Fibrinogen Btnd1Ng Sites On Human Platelets Using Photoaffinity Techniques: Some Preliminary Findings

1981 ◽  
Author(s):  
Ellinor I Peerschke ◽  
Mariorie B Zucker ◽  
Avner Rotman
Keyword(s):  
Molecular Weight ◽  
Apparent Molecular Weight ◽  
Human Platelets ◽  
Platelet Membrane ◽  
Membrane Fragment ◽  
Fibrinogen Receptor ◽  
Congenital Deficiency ◽  
Sds Page ◽  
Platelet Membrane Receptor

The interaction of fibrinogen with its, platelet membrane receptor was investigated using 125-labeled fibrinogen which was photoaffinity labeled with a light-sensitive azide. This photoreactive material (125I-NPA-fibr) was indistinguishable from unlabeled fibrinogen as well as from iodinated fibrinogen on SDS-PAGE. It bound specifically to platelets stimulated with ADP and was crosslinked to the platelet membrane after exposure to light ( λ >300 nm) for 4 min. No crosslinking was observed in the presence of EDTA or with platelets that failed to aggregate with ADP either due to the congenital deficiency thrombasthenia or following incubation with EDTA for 8 min at 37° , pH 7.8 and recalcification. SDS-PAGE of platelets bearing crosslinked 125I-NPA-fibr revealed a radiolabeled band of about 450,000 daltons in addition to the 340,000 dalton radioactive band of fibrinogen, suggesting that fibrinogen had been covalently bound to a platelet membrane component with an intact apparent molecular weight of approximately 110,000 daltons. Following reduction, an extra radioactive band was noted at 80,000 daltons. As the A∝-chains of fibrinogen were too weakly labeled to be detected by autoradiography, this indicated that either the Bβ or γchain of fibrinogen was attached to a 25,000-35,000 molecular weight platelet membrane fragment. We conclude that the additional radioactive bands observed after electrophoresis of platelets bearing specifically bound-photoaffinity labeled 125I-fibrinogen most likely represent the binding of the B β or γ chains of fibrinogen to the platelet fibrinogen receptor which may be GPIIb.

scholarly journals Isolation and Characterization of 2,3-Dichloro-1-Propanol-Degrading Rhizobia

2000 ◽  
Vol 66 (7) ◽  
pp. 2882-2887 ◽  
Author(s):  
Agus J. Effendi ◽  
Steven D. Greenaway ◽  
Brian N. Dancer
Keyword(s):  
Molecular Weight ◽  
High Ph ◽  
Molecular Weights ◽  
Isolation And Characterization ◽  
Complete Mineralization ◽  
Native Molecular Weight

ABSTRACT 2,3-Dichloro-1-propanol is more chemically stable than its isomer, 1,3-dichloro-2-propanol, and is therefore more difficult to degrade. The isolation of bacteria capable of complete mineralization of 2,3-dichloro-1-propanol was successful only from enrichments at high pH. The bacteria thus isolated were found to be members of the α division of the Proteobacteria in the Rhizobiumsubdivision, most likely Agrobacterium sp. They could utilize both dihaloalcohol substrates and 2-chloropropionic acid. The growth of these strains in the presence of 2,3-dichloro-1-propanol was strongly affected by the pH and buffer strength of the medium. Under certain conditions, a ladder of four active dehalogenase bands could be visualized from this strain in activity gels. The enzyme involved in the complete mineralization of 2,3-dichloro-1-propanol was shown to have a native molecular weight of 114,000 and consisted of four subunits of similar molecular weights.

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