An integrated microfluidic device in polyester for electrophoretic analysis of amino acids

2005 ◽  
Vol 26 (9) ◽  
pp. 1843-1848 ◽  
Author(s):  
Yanli Guo ◽  
Katsumi Uchiyama ◽  
Tatsuro Nakagama ◽  
Takuya Shimosaka ◽  
Toshiyuki Hobo
Keyword(s):  
Amino Acids ◽  
Microfluidic Device ◽  
Electrophoretic Analysis

scholarly journals Sampling and Electrophoretic Analysis of Segmented Flow Streams Using Virtual Walls in a Microfluidic Device

2008 ◽  
Vol 80 (21) ◽  
pp. 8231-8238 ◽  
Author(s):  
Gregory T. Roman ◽  
Meng Wang ◽  
Kristin N. Shultz ◽  
Colin Jennings ◽  
Robert T. Kennedy
Keyword(s):  
Microfluidic Device ◽  
Electrophoretic Analysis ◽  
Segmented Flow

Note. Effect of brining time on proteolytic changes in Idiazábal cheese during ripening / Nota. Cambios proteolíticos durante la maduración del queso Idiazábal por efecto del tiempo en salmuera

1996 ◽  
Vol 2 (5) ◽  
pp. 335-339 ◽  
Author(s):  
F.C. Ibáñez ◽  
A.I. Ordóñez ◽  
M.S. Vicente ◽  
M.I. Torres ◽  
Y. Barcina
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Total Nitrogen ◽  
Free Amino Acids ◽  
Free Amino ◽  
Dry Matter ◽  
Electrophoretic Analysis ◽  
Soluble Nitrogen ◽  
Clear Trend ◽  
Protein Nitrogen

Idiazábal cheeses were made employing brining times of 12 h (batch A) and 36 h (batch B). Proteolytic changes in both batches were examined over 270 d of ripening; proteolysis was low in both batches, but lower in batch B than in batch A. Electrophoretic analysis revealed incom plete breakdown of αs and β-caseins at the end of the ripening period, particularly in batch B. The proportion of soluble nitrogen as a percentage of total nitrogen was 17.55% in batch B and 19.48% in batch A, while the proportion of non-protein nitrogen was 11.78% in batch B and 15.16% in batch A. The proportion of non-protein nitrogen as a percentage of soluble nitrogen was 67.17% in batch B and 77.88% in batch A. The free amino acids, the smallest non-protein nitrogen frac tion, attained values of 1203 mg/100 g of dry matter in batch B and 1902 mg/100 g of dry matter in batch A. After 60 d of ripening, the main free amino acids were glutamic acid, valine, leucine, lysine, and phenylalanine in both batches, although levels were higher in the batch with the shorter brining time. There was no clear trend in the non-protein-forming amino acids with either ripening time or brining time.

Design, Fabrication of High-Throughput Microarray Microfluidic Device for Membrane Protein Polyhedra Formation

2011 ◽  
Author(s):  
Hsin-Jui Wu ◽  
Yiwei Yan ◽  
Y. C. Lee ◽  
Michael Stowell
Keyword(s):  
Drug Delivery ◽  
Amino Acids ◽  
Membrane Protein ◽  
Microfluidic Device ◽  
High Throughput ◽  
Human Body ◽  
Medical Technology ◽  
Variable Number ◽  
Functional Element ◽  
Variable Geometry

In this paper, we designed and fabricated High-throughput Microfluidic device for membrane protein polyhedral. Protein is the most important functional element in our human body and also it could be applied to the key application areas of drug bonding and drug delivery. However protein stucture is difficult to be analyzed due to the complex and variable geometry of protein stucture which can be randomly formed by 20 amino acids and also plused 3D folding of stucture possibly. Based on this, we could imagine it would be a huge variable number of protein stucture, let’s say billion possibilities. Therefore if we can successful discover protein stucture, then we can expect that will improve drug delivery of medical technology forward to a big step.

scholarly journals Mouse Ten-m/Odz Is a New Family of Dimeric Type II Transmembrane Proteins Expressed in Many Tissues

1999 ◽  
Vol 145 (3) ◽  
pp. 563-577 ◽  
Author(s):  
Toshitaka Oohashi ◽  
Xiao-Hong Zhou ◽  
Kang Feng ◽  
Brigitta Richter ◽  
Matthias Mörgelin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Alkaline Phosphatase ◽  
Transmembrane Protein ◽  
Transmembrane Proteins ◽  
Extracellular Domain ◽  
Electrophoretic Analysis ◽  
Type Ii ◽  
Mrna Isoforms ◽  
Hydrophobic Region ◽  
Hydrophobic Domain

The Drosophila gene ten-m/odz is the only pair rule gene identified to date which is not a transcription factor. In an attempt to analyze the structure and the function of ten-m/odz in mouse, we isolated four murine ten-m cDNAs which code for proteins of 2,700–2,800 amino acids. All four proteins (Ten-m1–4) lack signal peptides at the NH2 terminus, but contain a short hydrophobic domain characteristic of transmembrane proteins, 300–400 amino acids after the NH2 terminus. About 200 amino acids COOH-terminal to this hydrophobic region are eight consecutive EGF-like domains. Cell transfection, biochemical, and electronmicroscopic studies suggest that Ten-m1 is a dimeric type II transmembrane protein. Expression of fusion proteins composed of the NH2-terminal and hydrophobic domain of ten-m1 attached to the alkaline phosphatase reporter gene resulted in membrane-associated staining of the alkaline phosphatase. Electronmicroscopic and electrophoretic analysis of a secreted form of the extracellular domain of Ten-m1 showed that Ten-m1 is a disulfide-linked dimer and that the dimerization is mediated by EGF-like modules 2 and 5 which contain an odd number of cysteines. Northern blot and immunohistochemical analyses revealed widespread expression of mouse ten-m genes, with most prominent expression in brain. All four ten-m genes can be expressed in variously spliced mRNA isoforms. The extracellular domain of Ten-m1 fused to an alkaline phosphatase reporter bound to specific regions in many tissues which were partially overlapping with the Ten-m1 immunostaining. Far Western assays and electronmicroscopy demonstrated that Ten-m1 can bind to itself.

Highly resolved separation and sensitive amperometric detection of amino acids with an assembled microfluidic device

2009 ◽  
Vol 30 (9) ◽  
pp. 1490-1496 ◽  
Author(s):  
Chun Zhai ◽  
Wei Qiang ◽  
Jianping Lei ◽  
Huangxian Ju
Keyword(s):  
Amino Acids ◽  
Microfluidic Device ◽  
Amperometric Detection

scholarly journals Characterization of the development of cowpea cultivars and of the quantity and quality of proteins in their grains

2020 ◽  
Vol 55 ◽  
Author(s):  
Fabíola Vieira Gonçalves ◽  
Leonardo Oliveira Medici ◽  
Marcos Paulo Santos da Fonseca ◽  
Salete Aparecida Gaziola ◽  
Gepatrik Rodrigues Lima ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Content ◽  
Plant Development ◽  
Dry Matter ◽  
Protein Denaturation ◽  
Electrophoretic Analysis ◽  
Protein Band ◽  
Soluble Proteins ◽  
Cowpea Cultivars

Abstract: The objective of this work was to evaluate cowpea (Vigna unguiculata) cultivars regarding plant development and the quantity and quality of soluble proteins in their grains, for breeding purposes. The experiment was conducted in a greenhouse, in a completely randomized experimental design, with the Paulistinha, BRS Novaera, Epace 10, and BR 17-Gurguéia cultivars. Leaf area, shoot fresh and dry matter, leaf protein content, number of nodules, and nodule and root dry matter were evaluated. In mature grains, soluble fractions and soluble amino acids were also quantified, and the electrophoretic analysis was performed with protein denaturation. There were no differences between cultivars for the plant development variables. However, protein quantity and quality in the grain differed between cultivars. 'BRS Novaera' and 'BR 17-Gurguéia' showed a higher soluble protein content in their grains. 'BRS Novaera' exhibited higher contents of two soluble sulfur amino acids - methionine and cysteine - , not differing from 'BR 17-Gurguéia' regarding methionine content. Both cultivars presented protein band polymorphism, but BRS Novaera had an extra band for albumins. The BRS Novaera and BR 17-Gurguéia cultivars have the highest content of soluble proteins in their grains and the greatest protein polymorphism, which makes them suitable for improving the nutritional quality of cowpea.

Homochirality as the Signature of Extra-Terrestrial Life

1997 ◽  
Vol 161 ◽  
pp. 505-510
Author(s):  
Alexandra J. MacDermott ◽  
Laurence D. Barron ◽  
Andrè Brack ◽  
Thomas Buhse ◽  
John R. Cronin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Optical Rotation ◽  
Physical Origin ◽  
Natural Choice ◽  
Rosetta Mission ◽  
Terrestrial Life ◽  
Subsurface Layers ◽  
Solar System Bodies ◽  
Origin Of Homochirality

AbstractThe most characteristic hallmark of life is its homochirality: all biomolecules are usually of one hand, e.g. on Earth life uses only L-amino acids for protein synthesis and not their D mirror images. We therefore suggest that a search for extra-terrestrial life can be approached as a Search for Extra- Terrestrial Homochirality (SETH). The natural choice for a SETH instrument is optical rotation, and we describe a novel miniaturized space polarimeter, called the SETH Cigar, which could be used to detect optical rotation as the homochiral signature of life on other planets. Moving parts are avoided by replacing the normal rotating polarizer by multiple fixed polarizers at different angles as in the eye of the bee. We believe that homochirality may be found in the subsurface layers on Mars as a relic of extinct life, and on other solar system bodies as a sign of advanced pre-biotic chemistry. We discuss the chiral GC-MS planned for the Roland lander of the Rosetta mission to a comet and conclude with theories of the physical origin of homochirality.

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