scholarly journals Purification and on-column refolding of His-tagged PhaZ depolymerase from Pseudomonas putida KT2442 on Ni2+-NTA agarose gel: preparation of a novel immobilized biocatalyst

2009 ◽  
Vol 25 ◽  
pp. S122
Author(s):  
I. De La Mata ◽  
M. Arroyo ◽  
M. Villalón ◽  
J. García Hidalgo ◽  
M.A. Prieto ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Agarose Gel ◽  
Immobilized Biocatalyst ◽  
Gel Preparation

scholarly journals Automatic Lab on PCB System for Agarose Gel Preparation and Electrophoresis for Biomedical Applications

2021 ◽  
Author(s):  
Jesús David Urbano-Gámez ◽  
Francisco Perdigones ◽  
José Manuel Quero
Keyword(s):  
Biomedical Applications ◽  
Mixing Time ◽  
Dna Amplification ◽  
Agarose Gel ◽  
Curing Time ◽  
Agarose Gels ◽  
Conductivity Sensor ◽  
Ntc Thermistor ◽  
Gel Preparation ◽  
Maximum Voltage

In this paper, a prototype of an automatic lab on PCB for agarose preparation and electrophoresis is developed. The dimensions of the device are 38×34 mm2 and includes a conductivity sensor for detecting the TAE buffer (Tris-Acetate-EDTA buffer), a microheater for mixing, a NTC thermistor for controlling the temperature, a LDR sensor for measuring the transparency of the mixture, and two electrodes for performing the electrophoresis. The agarose preparation functions are governed by a microcontroller. The device requires a PMMA structure to define the wells of the agarose gel, and to release the electrodes from the agarose. The maximum voltage and current that the system requires are 40 V to perform the electrophoresis, and 1 A for activating the microheater. The chosen temperature for mixing is 80ºC, with a mixing time of 10 min. In addition, the curing time is about 30 min. This device is intended to be integrated as a part of a larger lab on PCB system for DNA amplification and detection. However, it can be used to migrate DNA amplified in conventional thermocyclers. Moreover, the device can be modified for preparing larger agarose gels and performing electrophoresis in an automatic manner.

scholarly journals Semi-Automatic Lab-on-PCB System for Agarose Gel Preparation and Electrophoresis for Biomedical Applications

Micromachines ◽  
2021 ◽  
Vol 12 (9) ◽  
pp. 1071
Author(s):  
Jesús David Urbano-Gámez ◽  
Francisco Perdigones ◽  
José Manuel Quero
Keyword(s):  
Biomedical Applications ◽  
Negative Temperature Coefficient ◽  
Mixing Time ◽  
Dna Amplification ◽  
Negative Temperature ◽  
Agarose Gel ◽  
Curing Time ◽  
Conductivity Sensor ◽  
Ntc Thermistor ◽  
Gel Preparation

In this paper, a prototype of a semi-automatic lab-on-PCB for agarose gel preparation and electrophoresis is developed. The dimensions of the device are 38 × 34 mm2 and it includes a conductivity sensor for detecting the TAE buffer (Tris-acetate-EDTA buffer), a microheater for increasing the solubility of the agarose, a negative temperature coefficient (NTC) thermistor for controlling the temperature, a light dependent resistor (LDR) sensor for measuring the transparency of the mixture, and two electrodes for performing the electrophoresis. The agarose preparation functions are governed by a microcontroller. The device requires a PMMA structure to define the wells of the agarose gel, and to release the electrodes from the agarose. The maximum voltage and current that the system requires are 40 V to perform the electrophoresis, and 1 A for activating the microheater. The chosen temperature for mixing is 80 ∘C, with a mixing time of 10 min. In addition, the curing time is about 30 min. This device is intended to be integrated as a part of a larger lab-on-PCB system for DNA amplification and detection. However, it can be used to migrate DNA amplified in conventional thermocyclers. Moreover, the device can be modified for preparing larger agarose gels and performing electrophoresis.

Luminography – an Alternative Assay for Detection of von Willebrand Factor Multimers

1988 ◽  
Vol 60 (02) ◽  
pp. 133-136 ◽  
Author(s):  
R Schneppenheim ◽  
H Plendl ◽  
U Budde
Keyword(s):  
Von Willebrand Factor ◽  
Gel Electrophoresis ◽  
Detection Methods ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Luminescence Assay ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryA luminescence assay was adapted for detection of von Willebrand factor multimers subsequent to SDS-agarose gel electrophoresis and electroblotting onto nitrocellulose. The method is as fast as chromogenic detection methods and appears to be as sensitive as autoradiography without the disadvantages of the latter.

Identification of Fibrinogen Derivatives in Plasma Samples

1972 ◽  
Vol 27 (03) ◽  
pp. 610-618 ◽  
Author(s):  
H Graeff ◽  
R von Hugo
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Gel Chromatography ◽  
Agarose Gel ◽  
Plasma Samples ◽  
Methodological Study ◽  
Parent Molecule ◽  
Electrophoretic Mobilities ◽  
Fibrin Monomer

SummaryThe observation of fibrinogen derivatives with a molecular weight higher than the parent molecule in human cases of DIC initiated the present methodological study. These derivatives were identified by the following methods : 2.5 M β-alanine precipitation of the plasma samples, PAA gel electrophoresis, intra gel immunoprecipitation and agarose gel chromatography. In the plasma of a patient with severe eclampsia and laboratory signs of DIC two derivatives with a molecular weight higher than that of fibrinogen were identified according to their relative electrophoretic mobilities: 0.18 and 0.28 × 10−5 cm2/V × sec (fibrinogen: 0.43 × 10−5 cm2/V × sec). Electrophoretic studies in the presence of 5 M urea indicated that the 0.28 derivative is a complex probably formed by fibrinogen and a fibrin monomer.

The Preparation and Evaluation of a Standardized Fibrin Plate for the Assessment of Fibrinolytic Activity

1970 ◽  
Vol 23 (02) ◽  
pp. 202-210 ◽  
Author(s):  
R Bishop ◽  
H Ekert ◽  
G Gilchrist ◽  
E Shanbrom ◽  
L Fekete
Keyword(s):  
Test Specimen ◽  
Fibrinolytic Activity ◽  
Clinical Laboratory ◽  
Fibrin Clot ◽  
Fibrinolytic Enzyme ◽  
Agarose Gel ◽  
Fibrin Plate ◽  
Percent Concentration ◽  
Human Plasminogen ◽  
Preparation And Evaluation

SummaryA new fibrin plate technic for evaluating components of the fibrinolytic system has been developed. It provides quick, accurate, and easily interpreted results for the fibrinolytic profile. The standardized human plasminogen-free fibrin plates can be produced in bulk and stored for prolonged periods of time. A test specimen placed in a well punched in the buffered agarose gel diffuses into the agar and lyses the fibrin clot, forming a clear reaction zone. The zone diameter is directly proportional to the log of the percent concentration of available fibrinolytic enzyme in the specimen. The plates may be used to quantitate total plasminogen, and estimate available plasmin and active plasmin. A good correlation between results obtained using these fibrin plates and caseinolytic methods was found. Performance and interpretation of tests of fibrinolysis done on these new fibrin plates indicate that it may be the most sensitive technic available for clinical laboratory work.

Enzimaktivitások és a fluoreszkáló pszeudomonasz csíraszámok változása a fehér lóhere (Trifolium repens L.) rizoszférájában sókezelés (NaCl) hatására

2004 ◽  
Vol 53 (3-4) ◽  
pp. 367-376 ◽  
Author(s):  
A. A. Khalif ◽  
H. Abdorhim ◽  
Hosam E. H. T. Bayoumi ◽  
Anna Füzy ◽  
Mihály Kecskés
Keyword(s):  
Pseudomonas Putida ◽  
Trifolium Repens ◽  
Trifolium Repens L

Üvegházi körülmények között savanyú barna erdotalajban nevelt fehér here (Trifolium repens L.) növények rizoszférájának sókezelés hatására bekövetkezo változását ellenoriztük. Megvizsgáltuk a különbözo sókoncentrációknak (0, 0,2, 0,4, 0,6 és 0,8 tömeg %) a baktériumnépesség összetételére és a különbözo talajenzimek aktivitására gyakorolt hatását.  Megállapítottuk, hogy a talaj sótartalma közvetlenül befolyásolta a rizoszférában található fluoreszkáló pszeudomonaszok csíraszámát. A legsurubb populáció a 0,2% NaCl-ot tartalmazó talajban volt mérheto, ahol a fluoreszkáló pszeudomonaszok között a Pseudomonas putida és a P. fluorescens fordultak elo a legnagyobb számban. A pszeudomonaszok ily módon jól tolerálják a talaj magas NaCl-tartalmát, és gyökérkolonizáló tevékenységet képesek kifejteni a magas NaCl-tartalmú talajban is. A sókoncentráció növelésével kezdetben (a 0,2-0,4%-os tartományban) jelentosen növekedett a dehidrogenáz, kataláz, és ureáz enzimek aktivitása. A proteáz enzimek aktivitásmaximuma a 0,1-0,2% NaCl-koncentráció tartományba esett. A 0,4%-nál magasabb koncentrációkban a kontrollhoz hasonló mértékure csökkent mind a négy enzim aktivitása, és a baktériumok száma is. A foszfatáz- és a b-glükozidáz-tevékenység viszont a NaCl-dózis növelése következtében a koncentrációval arányosan, jelentosen csökkent a kontrollhoz viszonyítva.  Feltételezésünk szerint az enzimaktivitások változását is a sókezelés hatására bekövetkezo mikrobióta összetételének megváltozása okozta.

Exemplar Abstract for Pseudomonas putida (Trevisan 1889) Migula 1895 (Approved Lists 1980).

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Pseudomonas Putida
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