PSVI-26 Optimized small tissue specific protein isolation trough complexed diafiltration technique

2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 387-388
Author(s):  
Kotenkova Elena ◽  
Irina M Chernukha ◽  
Leonid I Kovalyov
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Raw Material ◽  
Fatty Acid Binding Proteins ◽  
Separation And Purification ◽  
Fatty Acid Binding ◽  
Tissue Specific ◽  
Isolation And Purification ◽  
Small Tissue ◽  
Mass Spectrometry Identification

Abstract Physiologically active and pure small tissue specific proteins are in demand in various fundamental and applied areas due to its bioactive properties. It is known that proteins can aggregate, as well as form a highly concentrated layer at the border of the filtration membrane or adhere to it, which significantly interferes with filtration. To eliminate these effects, protein-peptide extracts are recommended to be diluted, as well as using special agents, among them amino acids are more suitable for food industry. The purpose of the study is to develop the isolation and purification of proteins with molecular weight lower 50kDa from porcine hearts and aortas, using different amino acids and its combination. It was previously revealed, that family of fatty acid binding proteins (FABP) is one of the most stable and physiologically active protein in such raw materials. The final technology includes extraction, centrifugation, dilution of extract, diafiltration, lyophilization, dissolving in a small volume of distilled water, dialization and final drying. Concentration of 1.0% glycine and 0.1M proline in both diluted extract and exchange solution was revealed to be most effective to prevent protein aggregation. Dialysates were dried lyophilically and O’Farrell 2DE-electrophoresis with MALDI-TOF MS and MS/MS mass spectrometry identification were used. No proteins of 50kDa and bigger were detected. Proteins of lipid metabolism, peroxiredoxin 2, transgelins etc. with molecular weight lower 50kDa were found. The developed technology allows increasing cardiac and adipocytic isoforms of FABP family content. Cardiac isoform was previously identified in raw material, while adipocytic was newly detected. Adipocytic isoform content is lower than cardiac one; therefore, it was not detected in raw material, but application of complexed diafiltration technique led to increasing its content in dialysate. The developed technology can be used for separation and purification of animal proteins in native and stable forms.

Sequence of fatty acid binding proteins and their tissue-specific expression in adult zebrafish (Danio rerio)

2000 ◽  
Vol 28 (5) ◽  
pp. A238-A238
Author(s):  
J. M. Wright ◽  
E. M. Denovan-Wright ◽  
M. Pierce ◽  
Y. Wang ◽  
M. K. Sharma ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Danio Rerio ◽  
Binding Proteins ◽  
Fatty Acid Binding Proteins ◽  
Adult Zebrafish ◽  
Specific Expression ◽  
Fatty Acid Binding ◽  
Tissue Specific ◽  
Tissue Specific Expression

scholarly journals Albumin, as a Therapeutic Protein: Potential Source, Application, Isolation and Purification

2021 ◽  
Vol 12 (3) ◽  
pp. 1922-1931
Author(s):  
Ukun MS Soedjanaatmadja ◽  
Nadiya Adnani ◽  
Wildan Abiyyi ◽  
Saadah Diana Rachman ◽  
Shabarni Gaffar ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Plasma Viscosity ◽  
Normal Serum ◽  
High Yield ◽  
Molecular Forms ◽  
Single Chain ◽  
Isolation And Purification ◽  
Pangasianodon Hypophthalmus ◽  
Potential Source

Albumin is one of the plasma proteins found in the human body, which is about 55-60%, and the total normal serum protein level is 3.8-5.0 g/dL. Albumin consists of a single chain of a polypeptide with a molecular weight of 66.5kDa and consists of 585 amino acids. In the albumin molecule, 17 disulfide bonds connect amino acids containing sulfur. The molecular albumin is elliptical so that with such molecular forms, it will not increase the plasma viscosity and dissolve perfectly. Albumin is protein and its action as a transport agent and maintains colloid osmotic pressure. The need for albumin in the world reaches 500 tons annually, which is used hypoalbuminemia therapy. Hypoalbuminemia therapy which is often used is HSA (Human Serum Albumin) therapy. The use of HSA has disadvantages such as causing infections, expensive processing costs, and the cost of products. Thus other sources of albumin are needed. One that can be the potential source of albumin is Indonesian catfish (Clariasgariepinus). Our research studies have obtained the albumin from Indonesian catfish (C. gariepinus) and Patin fish (Pangasianodon hypophthalmus) with high yield and purity. The Indonesian catfish is the potential albumin source after the isolation and purification process was obtained that the molecular weight, the purity, and the total albumin content of purified albumin were 66.7 kDa, 95.38%, and 118.5 mg /g of wet weight, respectively.

scholarly journals Small Bowel Review - Part I

1997 ◽  
Vol 11 (6) ◽  
pp. 515-531 ◽  
Author(s):  
ABR Thomson ◽  
G Wild
Keyword(s):  
Amino Acids ◽  
Small Bowel ◽  
Brush Border Membrane ◽  
Sugar Transport ◽  
Fatty Acid Binding Proteins ◽  
Fatty Acid Binding ◽  
Oral Rehydration ◽  
Membrane Hydrolysis ◽  
Intracellular Metabolism ◽  
Made In

Significant advances have been made in the study of the small bowel. Part I of this two-part review of the small bowel examines carbohydrates, including brush border membrane hydrolysis and sugar transport; amino acids, dipeptides, proteins and food allergy, with a focus on glutamine, peptides and macromolecules, and nucleosides, nucleotides and polyamines; salt and water absorption, and diarrhea, including antidiarrheal therapy and oral rehydration treatment; lipids (digestion and absorption, fatty acid binding proteins, intracellular metabolism, lipoproteins and bile acids); and metals (eg, iron) and vitamins.

Organ-specific isoform selection of fatty acid–binding proteins in tissue-resident lymphocytes

2020 ◽  
Vol 5 (46) ◽  
pp. eaay9283 ◽  
Author(s):  
H. Frizzell ◽  
R. Fonseca ◽  
S. N. Christo ◽  
M. Evrard ◽  
S. Cruz-Gomez ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Immune Responses ◽  
The Body ◽  
Fatty Acid Binding Proteins ◽  
Common Mechanism ◽  
Fatty Acid Binding ◽  
Tissue Specific ◽  
Organ Specific ◽  
New Location ◽  
Selection Of

Tissue-resident memory T (TRM) cells exist throughout the body, where they are poised to mediate local immune responses. Although studies have defined a common mechanism of residency independent of location, there is likely to be a level of specialization that adapts TRM cells to their given tissue of lodgment. It has been shown that TRM cells in the skin rely on the uptake of exogenous fatty acids for their survival and up-regulate fatty acid–binding protein 4 (FABP4) and FABP5 as part of their transcriptional program. However, FABPs exist as a larger family of isoforms, with different members selected in a tissue-specific fashion that is optimized for local fatty acid availability. Here, we show that although TRM cells in a range of tissue widely express FABPs, they are not restricted to FABP4 and FABP5. Instead, TRM cells show varying patterns of isoform usage that are determined by tissue-derived factors. These patterns are malleable because TRM cells relocated to different organs modify their FABP expression in line with their new location. As a consequence, these results argue for tissue-specific overlays to the TRM cell residency program, including FABP expression that is tailored to the particular tissue of TRM cell lodgment.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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