scholarly journals Profil Protein Ikan Gurami (Osphronemus Gouramy) Sebelum dan Sesudah Penggaraman Berbasis SDS-PAGE

2019 ◽  
Vol 2 (1) ◽  
pp. 126
Author(s):  
Suardi Suardi ◽  
Ana Hidayanti Mukarromah ◽  
Stalis Norma Ethica
Keyword(s):  
Molecular Weight ◽  
Salt Concentration ◽  
Gel Electrophoresis ◽  
Research Method ◽  
Salt Content ◽  
Animal Protein ◽  
Fish Protein ◽  
Potential Source ◽  
Sds Page ◽  
Electrophoresis Method

Fish is a potential source of animal protein, but has a weakness that is easy to rot. To avoid decay can be preserved by salting the fish. In this study wet salting was carried out to analyze the effect of salting on fish protein. The sample used was a type of gourami with 5 tails. 1 for the sample before salting and 4 for salting each salted at 10, 20, 30 and 40% b/v after that it was left to stand for 12 hours. The research method used was the Gel Electrophoresis method (SDS-PAGE) to determine molecular weight (MW), looking at the purity and damage of proteins in the sample. The samples of gouramy before salting showed 16 bands, 8 major bands and 8 minor ribbons. Samples of gouramy with a salt concentration of 10% b/v showed 16 bands, 7 major bands and 9 minor bands. Samples of gouramy with a salt concentration of 20% b/v showed 14 bands, 7 major bands and 7 minor bands. Samples of gouramy with a salt concentration of 30% b/v showed 10 bands, 3 major bands and 7 minor bands. Samples of gouramy with a salt concentration of 40% b/v showed 9 bands, 3 major bands and 6 minor bands. Thus it can be concluded that salting of fish can affect the gouramy protein, which is the higher the salt content added, the protein found in the fish will be denatured. The salting process of 10% b/v in gouramy meat is the most recommended salting process compared to the salting process of 20, 30 and 40% b/v.Ikan merupakan sumber protein hewani yang potensial, namun memiliki suatu kelemahan yaitu mudah membusuk. Untuk menghindari pembusukan dapat dilakukan pengawetan dengan penggaraman pada ikan. Pada penelitian ini dilakukan penggaraman basah untuk menganalisis pengaruh penggaraman terhadap protein ikan. Sampel yang digunakan adalah jenis ikan gurami sebanyak 5 ekor. 1 ekor untuk sampel sebelum penggaraman dan 4 ekor dilakukan penggaraman masing-masing digarami dengan kadar 10, 20, 30 dan 40% b/v setelah itu didiamkan selama 12 jam. Metode penelitian yang digunakan adalah metode Elektroforesis Gel (SDS- PAGE) untuk menentukan berat molekul (BM), melihat kemurnian dan kerusakan protein pada sampel. Pada sampel ikan gurami sebelum penggaraman menunjukkan 16 pita, 8 pita mayor dan 8 pita minor. Sampel ikan gurami dengan konsentrasi garam 10% b/v menujukkan 16 pita, 7 pita mayor dan 9 pita minor. Sampel ikan gurami dengan konsentrasi garam 20% b/v menunjukkan 14 pita, 7 pita mayor dan 7 pita minor. Sampel ikan gurami dengan konsentrasi garam 30% b/v menunjukkan 10 pita, 3 pita mayor dan 7 pita minor. Sampel ikan gurami dengan konsentrasi garam 40% b/v menunjukkan 9 pita, 3 pita mayor dan 6 pita minor. Dengan demikian dapat disimpulkan bahwa penggaraman pada ikan dapat berpengaruh terhadap protein ikan gurami yaitu makin tinggi kadar garam yang ditambahkan maka protein yang terdapat pada ikan akan terdenaturasi. Proses penggaraman 10% b/v pada daging ikan gurami merupakan proses penggaraman yang paling disarankan dibandingkan proses penggaraman 20,30 dan 40% b/v.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

Study on Degradation of Radix Isatidis Polypeptide in Artificial Gastrointestinal Environment

2014 ◽  
Vol 989-994 ◽  
pp. 1020-1024
Author(s):  
Nan Nan ◽  
Xi Jing Liu
Keyword(s):  
Gel Electrophoresis ◽  
Free Amino ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Radix Isatidis ◽  
Sds Page ◽  
Electrophoresis Method ◽  
Amino Acid Levels ◽  
Different Molecular Weight

Radix Isatidis is a traditional Chinese medicine for treatment of influenza and inflammation in China. In this paper, in order to study the degradation situation of Radix Isatidis polypeptide in artificial gastrointestinal environment, the SDS-PAGE (Sodium dodecyl sulfate-polyacrylamide gel electrophoresis) method was used to detect the degradation of Radix Isatidis polypeptide in artificial intestinal juice and gastric juice, and it showed that Radix Isatidis peptides could be degradated to different degrees. HPLC (High Performance Liquid Chromatography) was used to determine the change of peptides degradation, and it indicated that free amino acid levels did not change significantly. The result after degradation was also detected by BCA method, and it showed that there were still a large number of polypeptides in the liquid. From this experiment we can come to this conclusion that Radix Isatidis polypeptides in artificial gastrointestinal juice mostly degraded into a series of different molecular weight peptides.

Catabolism of streptokinase and polyethylene glycol-streptokinase: evidence for transport of intact forms through the biliary system in the mouse

Blood ◽  
1990 ◽  
Vol 76 (1) ◽  
pp. 73-79 ◽  
Author(s):  
FH Brucato ◽  
SV Pizzo
Keyword(s):  
Molecular Weight ◽  
Polyethylene Glycol ◽  
Gel Electrophoresis ◽  
Proteinase Inhibitors ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gi Tract ◽  
Substantial Fraction ◽  
Sds Page ◽  
Derivatives Of

Abstract The catabolism of streptokinase (SK) and polyethylene glycol derivatives of SK (PEG-SK) were studied in mice. The clearance and catabolism of SK:plasmin (SK:Pm) and PEG-SK:Pm activator complexes were also investigated. Native 125I-SK cleared rapidly (t1/2 = 15 minutes) from the circulation, with the majority of the ligand accumulating in the liver and gastrointestinal (GI) tract and a substantial fraction also localizing in the kidneys. SK, which was removed from the plasma by the liver, was secreted into bile and then the GI tract. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that 125I-SK recovered from liver and bile was homogeneous and of the same molecular weight (mol wt approximately 50,200) as native SK. PEG-125I-SK cleared slowly (t1/2 greater than 200 minutes), with more than 80% of the preparation localizing in liver and GI tract. The PEG-125I-SK secreted into the bile was also intact. The bile containing 125I-SK was incubated with stoichiometric amounts of plasminogen and electrophoresed under nondenaturing conditions. This study demonstrated that the secreted SK was able to form SK:Pg complexes. SDS-PAGE also showed activation of 125I-Pg that was incubated with recovered bile containing the SK. 125I-SK:Pm catabolism was also studied. In these experiments, the mol wt approximately 42,000 fragment obtained when SK is cleaved by plasmin was found in the bile. This fragment of 125I-SK was not recovered as part of a complex with plasmin, consistent with our previous observations that catabolism of SK:Pm involves transfer of the plasmin to plasma proteinase inhibitors while SK is catabolized independently. By contrast, when PEG-125I-SK:Pm was injected into mice, only intact PEG-125I-SK was found in the bile, consistent with our previous observations that the PEG derivatization blocks its degradation by plasmin.

scholarly journals Serological grouping ofTreponema hyodysenteriae

1990 ◽  
Vol 105 (1) ◽  
pp. 79-85 ◽  
Author(s):  
D. J. Hampson ◽  
J. R. L. Mhoma ◽  
B. G. Combs ◽  
J. I. Lee
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Vaccine Development ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cross Reactivity ◽  
Low Molecular Weight ◽  
Serological Response ◽  
Double Immunodiffusion ◽  
Sds Page ◽  
Treponema Hyodysenteriae

SUMMARYTwo Australian isolates ofTreponema hyodysenteriaewhich did not fit within the current serological grouping system for these bacteria wrere examined by agarose gel double immunodiffusion tests (AGDP). Isolate Vic1 was serologically unique, and we propose that it becomes the type organism for a new sixth serological group ofT. hyodysenteriae(Group F). Isolate Q1 was unusual in that lipopolysaccharide (LPS) extracted from it reacted strongly in AGDP with serum raised against the type organism for serogroup D (A1), and also weakly with serum raised against the type organism for serogroup B (WA1). The nature of this cross-reactivity was examined by using cross-absorbed antisera in AGDP, and by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.The pattern of serological cross-reactivity between Q1, A1 and WA1 was complex and was not fully defined, but the isolate Q1 apparently shared low molecular weight ‘serogroup’ LPS antigens with A1, and shared higher molecular weight LPS antigens with WA1. On this basis Q1 was designated as belonging to serogroup D, although it was recommended that this be qualified as D (B) to indicate the presence of weak cross-reactivity with serogroup B. Such serological cross-reactivity may have significance in relation to the development of immunity toT. hyodysenteriae. Isolate Q1 may be a potentially useful organism for vaccine development because of its ability to induce a good serological response to LPS of treponemes from both serogroups D and B.

scholarly journals SIMPLE METHOD FOR OPTIMIZATION OF HEPARIN AND ENOXAPARIN DETECTION USING AGAROSE GEL ELECTROPHORESIS

2019 ◽  
pp. 12-15
Author(s):  
Ahmad Abdulrahman Almeman
Keyword(s):  
Molecular Weight ◽  
Toluidine Blue ◽  
Gel Electrophoresis ◽  
Optimization Procedure ◽  
Solvent Mixture ◽  
Acid Mixture ◽  
Low Molecular Weight ◽  
Simple Method ◽  
Electrophoresis Method ◽  
Tools And Techniques

Objective: A simple gel electrophoresis method for low-molecular-weight heparins (LMWH) is required for use in a variety of laboratories to allow further identification and purification. This study aimed to optimize the detection of heparin and enoxaparin (low-molecular-weight heparin by gel electrophoresis. Methods: Several gel electrophoresis conditions were tested to optimize the detection of enoxaparin by using a simple method with a modified Volpi’s approach. Multiple gel thicknesses, voltage settings, and enoxaparin concentrations were tested in the optimization procedure. Enoxaparin was purchased from a local supplier as pre-filled pharmaceutical injections. Highly purified 0.5% and 1.0% agarose gels were prepared and a series of enoxaparin concentrations was added to both gels for comparison and optimization. The 0.2% toluidine blue stain was prepared by the addition of 1 ml in an ethanol-water-acetic acid mixture (50:49:1; v/v/w). The staining process comprised two steps: first, toluidine blue was added for 30 min and destained overnight in the solvent mixture. Subsequently, the following morning, the second step was conducted, in which the gel was restained for 30 min with the same concentration of toluidine blue. We continued to stain the gel until the bands were visible. Results: The gel electrophoresis results showed that clearest and sharpest bands were obtained using 65–75 mAh and 85 V settings. At 95 mAh, the bands were slightly washed out. Conclusion: This study successfully facilitated the detection of enoxaparin, a LMWH, and heparin in the laboratory by using simple tools and techniques available in most laboratories.

Extraction of Keratin from Chicken Feather and Electrospinning of the Keratin/PLA Blends

2013 ◽  
Vol 747 ◽  
pp. 711-714 ◽  
Author(s):  
Siriorn Isarankura Na Ayutthaya ◽  
Jatuphorn Woothikanokkhan
Keyword(s):  
Molecular Weight ◽  
Ir Spectrum ◽  
Gel Electrophoresis ◽  
Electrospun Fiber ◽  
Electrospinning Process ◽  
Chicken Feather ◽  
Feather Waste ◽  
Sds Page ◽  
Ft Ir ◽  
Chicken Feather Waste

Keratins were extracted from chicken feather waste by sulphitolysis method, using various sodium metabisulphite contents. The extracted keratin was characterized by FT-IR and gel electrophoresis (SDS-PAGE) techniques. The extracted keratin with the highest molecular weight (12-20 kDa) was then selected for further study on electrospinning. The keratin/PLA solutions with a variety of blending ratios (10/90 to 90/10 w/w) were prepared before fabrication by electrospinning process. Morphology of the electrospun fiber was examined by using SEM technique, From the results, it was found that keratin/PLA blends containing 90 %wt of keratin could not be electrospun into fiber. By decreasing the keratin content to below 70 %wt, the blend solution can be electrospun into fiber. FT-IR spectrum of the keratin/PLA fiber showed the presence of peaks representing both keratin and PLA. These results confirmed that the fiber composed of both polymeric phases.

scholarly journals Mapping of the genes controlling high-molecular-weight glutelin subunits of rye on the long arm of chromosome 1R

1984 ◽  
Vol 44 (2) ◽  
pp. 117-123 ◽  
Author(s):  
N. K. Singh ◽  
K. W. Shepherd
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Translocation Line ◽  
Sds Page ◽  
Chromosome 1R

SUMMARYThe gene(s) controlling the high-molecular-weight glutelin subunits in rye (designated as Glu-Rl) was mapped with respect to the centromere using a 1RL-1DS wheat-rye translocation line and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Analysis of 479 seeds from test-crosses between a 1R/1RL-1DS heterozygote and the cultivar India 115, revealed 14·6% aneuploid and 3·95% recombinant progeny. Excluding the aneuploids, this locus was calculated to be 4·65 ± 1·04 cM from the centromere on the long arm of chromosome 1R, which is comparable to the position of the homoeologous loci in wheat and barley.

scholarly journals Identification of the platelet-specific alloantigen, Naka, on platelet membrane glycoprotein IV

Blood ◽  
1990 ◽  
Vol 75 (3) ◽  
pp. 684-687 ◽  
Author(s):  
Y Tomiyama ◽  
H Take ◽  
H Ikeda ◽  
T Mitani ◽  
T Furubayashi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Two Dimensional ◽  
Definitive Evidence ◽  
Sds Page ◽  
Platelet Transfusions

We describe the membrane localization of a new platelet-specific alloantigen, designated Naka, that is involved in refractoriness to HLA- matched platelet transfusions. By indirect immunoprecipitation, anti- Naka antibody precipitated a single, radiolabeled platelet membrane protein with a molecular weight (mol wt) of 91 Kd from Naka-positive platelets. When radiolabeled Naka-negative platelets were used as a source of target antigens, no radiolabeled proteins were precipitated. The analyses using nonreduced-reduced two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and using rabbit antiglycoprotein (GP)IV demonstrated that this protein corresponds to GPIV (alternatively GPIIIb). Furthermore, in dot immunobinding, anti- Naka antibody bound to purified GPIV. Our results provide definitive evidence that the Naka alloantigen is carried on GPIV. These results also demonstrate that, on occasion, antibodies against GPIV may play an important role in refractoriness to platelet transfusions.

scholarly journals MOLECULAR WEIGHT PROFILE OF PROTEASE OF PINEAPPLE (Ananas comosus L.Merr) AND PAPAYA (Carica papaya L.) USING SDS-PAGE METHOD

2017 ◽  
Vol 13 (1) ◽  
pp. 52
Author(s):  
Rizky Arcinthya Rachmania ◽  
Priyo Wahyudi ◽  
Aniza Mutia Wardani ◽  
Dini Rohmatul Insani
Keyword(s):  
Molecular Structure ◽  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Carica Papaya ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Ananas Comosus ◽  
Sds Page ◽  
Papaya Latex ◽  
Pharmaceutical Industries

<p>A group of protease enzymes such as papain and bromelain is able to decipher the molecular structure of the protein into amino acids which will be very useful in many fields, especially in food and pharmaceutical industries. The objective of this study to determine the molecular weight profile of enzyme bromelain from pineapple bark (<em>Ananas comosus</em> L. Merr) and papain (<em>Carica papaya</em> L.) from papaya latex with different varieties using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The precipitation was performed with ammonium sulfate ((NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub>)) 60 % addition and dialysized using a cellophane tubing with a pore size of 12,000 Dalton. The molecular weight of enzyme solution were determined using SDS-PAGE. The analysis results of molecular weight of enzyme bromelain of Subang and Bogor varieties were not different and were about 30.654 kDa, as well as the molecular weight of enzyme papain and Sukma California varieties were also not different and were about 23.485 kDa. It can be concluded that the different varieties of fruit of pineapple and papaya had no effect on the molecular weight of enzyme papain and bromelain.</p>

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