WO2010043668A1 - Points de sang séché pour une analyse de sang - Google Patents

Points de sang séché pour une analyse de sang Download PDF

Info

Publication number
WO2010043668A1
WO2010043668A1 PCT/EP2009/063470 EP2009063470W WO2010043668A1 WO 2010043668 A1 WO2010043668 A1 WO 2010043668A1 EP 2009063470 W EP2009063470 W EP 2009063470W WO 2010043668 A1 WO2010043668 A1 WO 2010043668A1
Authority
WO
WIPO (PCT)
Prior art keywords
filter paper
blood
cellulosic filter
blood sample
degradable
Prior art date
Application number
PCT/EP2009/063470
Other languages
English (en)
Inventor
Maryline Dumoulin
Isabelle Kreins
Jean-Claude Havaux
Alain Bosseloir
Original Assignee
Zentech S.A.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Zentech S.A. filed Critical Zentech S.A.
Publication of WO2010043668A1 publication Critical patent/WO2010043668A1/fr

Links

Classifications

    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N1/00Sampling; Preparing specimens for investigation
    • G01N1/28Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N1/00Sampling; Preparing specimens for investigation
    • G01N1/28Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q
    • G01N1/286Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q involving mechanical work, e.g. chopping, disintegrating, compacting, homogenising
    • G01N2001/2873Cutting or cleaving
    • G01N2001/288Filter punches
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/483Physical analysis of biological material
    • G01N33/487Physical analysis of biological material of liquid biological material
    • G01N33/49Blood

Definitions

  • the present invention relates to a method for analyzing blood samples from dried blood spots on filter paper.
  • the invention also relates to the use of cellulase for the digestion or degradation of the cellulosic filter paper.
  • Dried blood spot or DBS method consists of blotting few drops of blood onto a paper especially designed to absorb blood drops for laboratory analysis. Blood drops are obtained thanks to a light incision carried out to the heel or the ear lobe.
  • This method is slightly invasive and generally painless. This is the standard procedure when dealing with newborn diagnosis in paediatrics, prenatology or neonatology.
  • the use of paper cards, such as Guthrie card, for the collection of blood sample is particularly suitable for the storage and transport of blood samples at the time of epidemiologic studies or of screening of population. These cards are usually filter paper made of cotton linters. Other well-known advantages of this method are the ease of collection, the low volume of storage, and the transport without need for refrigeration.
  • the traditional method for newborn testing starts with the collection of a small amount of blood from newborn within the first postnatal days.
  • the sample is absorbed onto a piece of filter paper to provide a dried blood spot.
  • This sample is sent to the laboratory, where a small disk is punched out from the spot and loaded into a multiwell plate, where it is extracted with various solvents.
  • a sample might first be immersed for several hours in a methanol solution.
  • the sample is analyzed by standard spectroscopic methods, e.g. mass spectroscopy, high performance liquid chromatography or gas chromatography. The extraction is necessary since the paper piece which has been used for blood collection is still present in the multiwell plate.
  • the extraction step causes several drawbacks.
  • the degradation of the filter paper has been studied.
  • US 5,432,097 discloses the use of specific enzyme to digest the filter paper.
  • the degradation of the filter paper is partial and the supernatant have to be extracted at least four times from the compacted paper underlayer. Therefore, there is a need for the analysis of dried blood spots without resort to filtration or extraction step. There exits the need to circumvent the presence of the paper card and to allow efficient and fast testing of blood samples.
  • the inventors realised that providing a method comprising the entire degradation of the cellulosic filter paper can greatly improve the efficiency of the standard procedure.
  • the present invention relates to a method for analyzing blood sample from dried blood spots on filter paper comprising the steps of: a) providing a degradable cellulosic filter paper, b) placing a blood sample on said degradable cellulosic filter paper, c) drying said blood sample on said degradable cellulosic filter paper, thus providing a dried blood spot, d) punching out a small disc of said dried blood spot and moving it to a reaction vessel, e) degrading said degradable cellulosic filter paper from said dried blood spot with a cellulase in presence of an aqueous acidic solution, thus providing a blood sample; and, f) analyzing said blood sample, wherein said cellulase is selected from the group comprising endoglucanase, exoglucanase, hemicellulase and/or beta-glucosidase.
  • said agitation of step e) reaches a speed value ranging from 300 to 900rpm.
  • the use of a combination of enzymes can dramatically improve the degradation of the cellulosic filter paper from the dried blood spot. Moreover, the degradation of the cellulosic filter paper does not alter the blood sample which can be normally used afterwards.
  • the complete digestion of the cellulosic filter paper avoids a filtration step in the process of blood sample analysis.
  • the dried blood spot can be automatically process in deep-well plates or similar reaction vessel, thus avoiding manual handling and potential contamination of the sample.
  • the method of the present invention improves the time needed for the analysis. Therefore, more samples can be handled and analyzed per hour or per day.
  • the degradation of the cellulosic filter paper can greatly be improved by a specific combination of an enzymatic process and a physical or chemical process.
  • the method may combine an enzymatic process and an ultrasound treatment.
  • Cellulase or Cellulytic enzymes are enzymes involved in hydrolyse of cellulose.
  • the term "1 ,4-beta-D-glucan cellobiohydrase or exoglucanase or cellobiohydrolase” refers to an enzyme of general class E. C. 3.2.1.91 (Enzyme Classification), which is able to perform the hydrolysis of cellulose end chain, thus releasing cellobiose units.
  • the term "endo-beta-1 ,4-glucanase, endoglucanase or endo-1 ,4-beta-D- glucan 4-glucanohydrolase” refers to an enzyme of general class E. C. 3.2.1.4 (Enzyme Classification), which is able to perform the endohydrolysis of (1 ⁇ 4)- ⁇ -D-glucosidic linkages in cellulose, lichenin and cereal ⁇ -D-glucans.
  • beta-glucosidase refers to an enzyme of general class E. C. 3.2.1.21 (Enzyme Classification), which is able to hydrolyse the terminal, non-reducing ⁇ - D-glucose residues with release of ⁇ -D-glucose.
  • degradation or digestion refers to break down polymeric macromolecules into their smaller building blocks.
  • the present invention relates to a method for analyzing blood sample from dried blood spot on filter paper comprising the steps of: a) providing a degradable cellulosic filter paper, b) placing a blood sample on said degradable cellulosic filter paper, c) drying said blood sample on said degradable cellulosic filter paper, thus providing a dried blood spot, d) punching out a small disc of said dried blood spot and moving it to a reaction vessel, e) degrading said degradable cellulosic filter paper from said dried blood spot with a cellulase in presence of an aqueous acidic solution and agitating said solution, thus providing a blood sample; and f) analyzing said blood sample; wherein said cellulase is selected from the group comprising endoglucanase, exoglucanase, hemicellulase and/or beta-glucosidase.
  • said aqueous acidic solution may reach a pH value ranging from 2.0 to 8.0.
  • the pH value of said aqueous acidic solution may range from 3.0 to 7.0, more preferably from 4.0 to 6.0.
  • the pH value of said aqueous acidic solution may be 4.0, 4.1 , 4.2, 4.3, 4.4, 4.5, 4.6, 4.7, 4.8, 4.9, 5.0, 5.1 , 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9 or 6.0, or a value in the range between any two of the aforementioned values.
  • the pH value may allow to adapt the activity of the cellulase enzyme and thus to reduce the process time to a minimum.
  • the agitation of the solution in step e) is preferably done at a speed value ranging from 300 to 900rpm and can be done using conventional shakers or agitators known in the art, capable of agitating a fluid containing container, reservoir, recipient, tube, EppendorfTM tube or bottle.
  • said aqueous acidic solution may have a concentration of at least 0.01 molar.
  • said degradable cellulosic filter paper may be degraded in an aqueous acidic solution of at least 0.1 molar.
  • said degradable cellulosic filter paper may be degraded in an aqueous acidic solution having a concentration ranging from 0.1 molar to 5 molar. More preferably, said degradable cellulosic filter paper may be degraded in an aqueous acidic solution having a concentration ranging from 0.1 molar to 3 molar.
  • said degradable cellulosic filter paper may be degraded in an aqueous acidic solution having a concentration of 0.1 , 0.5, 1.0, 1.5, 2.0, 2.5 or 3.0 molar, or a value in the range between any two of the aforementioned values.
  • said aqueous acidic solution may contain hydrochloric acid, hydrofluoric acid, perchloric acid, thiocyanic acid, nitrous acid, chromic acid, methanesulfonic acid, trifluoromethanesulfonic acid, sulphuric acid, nitric acid, acetic acid, phosphate buffer, phosphoric acid, bromic acid, hypochloric acid, sulfinic acid, sulfonic acid, fumaric acid or carboxylic acids of general formula R-C(O)OH wherein R is CH 3 , CH 2 NO 2 , CH 2 F, CH 2 CI, CH 2 Br, CH 2 I, CHCI 2 , CCI 3 , CF 3 , H, HO, C 6 H 5 , 0-O 2 NC 6 H 4 , p- O 2 NC 6 H 4 , m-O 2 NC 6 H 4 , 0-ClC 6 H 4 , P-CIC 6 H 4 , m-CIC 6
  • said aqueous acidic solution may contain hydrochloric acid, sulphuric acid, nitric acid, acetic acid, phosphate buffer, phosphoric acid, bromic acid, hypochloric acid, sulfinic acid, sulfonic acid, fumaric acid. More preferably, said aqueous acidic solution may contain hydrochloric acid, acetic acid or phosphate buffer.
  • said degradable cellulosic filter paper may be degraded in an aqueous acidic solution of at least 0.1 molar containing hydrochloric acid, acetic acid or phosphate buffer.
  • said degradable cellulosic filter paper may be degraded in an aqueous acidic solution having a concentration ranging from 0.1 molar to 5 molar and containing hydrochloric acid, acetic acid or phosphate buffer.
  • said degradable cellulosic filter paper may be degraded in an aqueous acidic solution having a concentration ranging from 0.1 molar to 3 molar and containing hydrochloric acid, acetic acid or phosphate buffer.
  • said degradable cellulosic filter paper may be degraded in an aqueous acidic solution having a concentration of 0.1 , 0.5, 1.0, 1.5, 2.0, 2.5 or 3.0 molar, or a value in the range between any two of the aforementioned values, and containing hydrochloric acid, acetic acid or phosphate buffer.
  • the degradation of said degradable cellulosic filter paper performed in step e) may occur at a temperature ranging from 30 0 C to 70 0 C.
  • the activity of the cellulase enzyme can be also adapted by modulating the temperature.
  • the degradation of said degradable cellulosic filter paper of step e) may occur at a temperature ranging from 37°C to 65°C, more preferably from 37°C to 60 0 C.
  • the degradation of said degradable cellulosic filter paper of step e) may occur at a temperature of 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 55, 56, 57, 58, 59 or 60 0 C, or a value in the range between any two of the aforementioned values.
  • the degradation of said degradable cellulosic filter paper may be performed for 1 to 120 minutes.
  • said degradation of said degradable cellulosic filter paper may be performed for 1 to 90 minutes, more preferably for 1 to 60 minutes.
  • said degradation of said degradable cellulosic filter paper may be performed for 1 , 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55 or 60 minutes, or a value in the range between any two of the aforementioned values.
  • cellulases may include cellulases from Penicillium, Trichoderma, Humicola, Fusarium, Thermomonospora, Cellulomonas, Clostridium and Aspergillus.
  • cellulases may be produced from Trichoderma fungi.
  • Trichoderma include Trichoderma reesei, Trichoderma longibrachiatum, Trichoderma viride, Trichoderma koningii.
  • said cellulase may be produced with a genetically modified fungus from Trichoderma reesei.
  • said degradable cellulosic filter paper from said dried blood spot may be degraded with a combination of exoglucanase, endoglucanase and beta- glucosidase enzymes.
  • said degradable cellulosic filter paper from said dried blood spot may be degraded with a cellulase sold under the trademark AccelleraseTM 1000 and supplied by Genencor.
  • the method may further comprise the step of submitting said degradable cellulosic filter paper to a physical or chemical treatment.
  • the method may further comprise the step of submitting said degradable cellulosic filter paper to a physical treatment.
  • This combination of an enzymatic and a chemical/physical process improve the degradation of the filter paper and reduce the time required for the analysis.
  • the term "physical treatment" may refer to the exposure of said cellulosic filter paper to ultrasound, magnetic field, ultraviolet, infrared, microwave, electrical field, freezing or heating.
  • the term "chemical treatment” may refer to contacting the degradable cellulosic filter paper with salts, detergent or oxidant (e.g. sodium hypochlorite, hydrogen peroxide).
  • salts e.g. sodium hypochlorite, hydrogen peroxide.
  • the method may further comprise the step of submitting said degradable cellulosic filter paper to an ultrasound treatment prior to step e) or simultaneous to step e). In another preferred embodiment, the method may further comprise the step of submitting said degradable cellulosic filter paper to an ultrasound treatment prior to step e). Alternatively, the method may further comprise the step of submitting said degradable cellulosic filter paper to an ultrasound treatment simultaneous to step e).
  • the combination of ultrasound with a cellulase can avoid the use of non- environmental friendly solvent or components.
  • Said ultrasound treatment may consist of submitting said degradable cellulosic filter paper to an ultrasound field at frequencies in the range of 1 to 1000 kHz.
  • said degradable cellulosic filter paper may be submitted to an ultrasound field at frequencies ranging from 10 to 500 kHz, more preferably from 50 to 250 kHz.
  • said degradable cellulosic filter paper may be submitted to an ultrasound field at frequencies of 50, 60, 70, 80, 90, 100, 1 10, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240 or 250 kHz, or a value in the range between any two of the aforementioned values.
  • said degradable cellulosic filter paper may be submitted to an ultrasound field for a reaction time ranging from 1 second to 5 minutes.
  • said degradable cellulosic filter paper may be submitted to an ultrasound field for a reaction time ranging from 1 second to 1 minute, more preferably from 1 second to 45 seconds.
  • said degradable cellulosic filter paper may be submitted to an ultrasound field for a reaction time of 1 , 5, 10, 15, 20, 25, 30, 35, 40 or 45 seconds, or a value in the range between any two of the aforementioned values.
  • said method may further comprise the step of adding to the reaction vessel magnetic beads and submitting said reaction vessel to a magnetic stirrer.
  • said blood sample provided in step e) may be analyzed to detect endocrine disorders, e.g. congenital hypothyroidism (TSH), congenital adrenal hyperplasia.
  • said blood sample provided in step e) may be analyzed to detect blood cell disorders such as glucose-6-phosphate dehydrogenase deficiency.
  • said blood sample provided in step e) may be analyzed to detect inborn errors of metabolism such as disorders of carbohydrate metabolism, disorders of amino acid and organic acid metabolism, disorders of fatty acid oxidation and mitochondrial metabolism, disorders of porphyrin metabolism, disorders of purine or pyrimidine metabolism, disorders of steroid metabolism, disorders of mitochondrial function, disorders of peroxisomal function.
  • disorders of carbohydrate metabolism may include galactosemia, glycogen storage disease, lactose intolerance, fructose intolerance (aldolase B deficiency), fructosuria (hepatic fructokinase deficiency), galactose epimerase deficiency, galactokinase deficiency or hyperglycerolemia (glycerol kinase deficiency).
  • Non limiting examples of “disorders of amino acid metabolism and organic acid metabolism” may include phenylketonuria, tyrosinemia (type I, Il or III), alcaptonuria, homocystinuria, histidinemia, maple syrup urine disease (MSUD type Ib or II), methylmalonic aciduria, non-ketonic hyperglycinemia type I (NKHI), hyperlysinemia, carbamyl phosphate synthetase I deficiency, ornithine transcarbamylase deficiency, N- acetylglutamate synthetase deficiency, argininosuccinic aciduria, hyperargininemia, citrullinemia, ornithine aminotransferase deficiency, cystinuria (Type I or II), heartnup disease or hyperammonemia-hyperornithinemia-homocitrullinuroa syndrome.
  • phenylketonuria type
  • Non limiting examples of “disorders of fatty acid oxidation and mitochondrial metabolism” may include very-long-chain acyl-CoA dehydrogenase deficiency (VLCAD), long-chain acyl-CoA dehydrogenase deficiency (LCAD), medium-chain acyl-CoA dehydrogenase deficiency (MCAD), short-chain acyl-CoA dehydrogenase deficiency (SCAD), carnitine translocase deficiency, carnitine palmitoyltransferase I (CPT I) deficiency or carnitine palmitoylransferase Il (CPT II) deficiency.
  • VLCAD very-long-chain acyl-CoA dehydrogenase deficiency
  • LCAD long-chain acyl-CoA dehydrogenase deficiency
  • MCAD medium-chain acyl-CoA dehydrogenase defici
  • Non limiting examples of “disorders of porphyrin metabolism” may include acute intermittent porphyria, congenital erythropoietic porphyria (CEP), erythropoietic protoporphyria (EPP), ALA dehydratase deficiency porphyria (ADP), hereditary coproporphyria (HCP), variegate porphyria (VP), porphyria cutanea tarda (PCT) or hepatoerythropoietic porphyria (HEP).
  • CEP congenital erythropoietic porphyria
  • EPP erythropoietic protoporphyria
  • ADP ALA dehydratase deficiency porphyria
  • HCP hereditary coproporphyria
  • VP variegate porphyria
  • PCT hepatoerythropoietic porphyria
  • Non limiting examples of “disorders of purine or pyrimidine metabolism” may include Lesch-Nyhan syndrome, severe combined immunodeficiency disease (SCID), gout, renal lithiasis, xanthinuria, orotic aciduria (type I or II), or ornithine transcarbamoylase deficiency.
  • Non limiting examples of “disorders of steroid metabolism” may include congenital adrenal hyperplasia, 21 -Hydroxylase deficiency or salt-losing congenital adrenal hyperplasia
  • Non limiting examples of “disorders of mitochondrial function” may include Kearns-Sayre syndrome or external ophthalmoplegia NOS.
  • Non limiting examples of "disorders of peroxisomal function” may include Zellweger syndrome, X-linked adrenoleukodystrophy, neonatal adrenoleukodystrophy (NALD), rhizomelic chondrodysplasia punctata (RCDP) or infantile Refsum's disease (IRD).
  • said blood sample provided in step e) may be analyzed to detect phenylketonuria.
  • said blood sample of step f) may be analyzed to detect maple syrup urine disease.
  • said blood sample of step f) may be analyzed to detect phenylketonuria and maple syrup urine disease.
  • said blood sample provided in step e) may contain lysed blood cells.
  • Lysed blood cells refer to blood cells having their cellular membrane deteriorated or broken.
  • the present invention is particularly useful for the degradation of cellulosic filter paper.
  • the use of a combination of endoglucanase, exoglucanase, hemicellulase and/or beta-glucosidase enzymes and/or ultrasound treatment is suitable for the degradation of cellulosic filter paper.
  • the use of endoglucanase, exoglucanase, beta-glucosidase enzymes and ultrasound treatment is particularly suitable for the degradation of cellulosic filter paper.
  • the present invention relates to a method for the analysis in parallel of a plurality of blood samples from dried blood spots comprising the steps of: a) providing a plurality of dried blood spots, b) punching out a small disc of said dried blood spots and moving each disc to a different well of a multiwell plate, c) degrading the dried blood spots with a cellulase in presence of an aqueous acidic solution, thus providing a plurality of blood samples, and d) analyzing said blood sample in parallel,
  • cellulase is selected from the group comprising endoglucanase, exoglucanase, hemicellulase and/or beta-glucosidase

Abstract

La présente invention porte sur un procédé pour analyser des échantillons sanguins à partir de points de sang séché sur un papier filtre. En particulier, le procédé de l'invention peut comprendre les étapes consistant à : a) fournir un papier filtre cellulosique dégradable, b) placer un échantillon sanguin sur ledit papier filtre cellulosique dégradable, c) sécher ledit échantillon sanguin sur ledit papier filtre cellulosique dégradable, fournissant ainsi un point de sang séché, d) découper un petit disque dudit point de sang séché et le déplacer vers un récipient de réaction, e) dégrader ledit papier filtre cellulosique dégradable à partir dudit point de sang séché avec une cellulase en présence d'une solution acide aqueuse, fournissant ainsi un échantillon sanguin et f) analyser ledit échantillon sanguin ; ladite cellulase étant choisie dans le groupe comprenant l'endoglucanase, l'exoglucanase, l'hémicellulase et/ou la bêta-glucosidase.
PCT/EP2009/063470 2008-10-17 2009-10-15 Points de sang séché pour une analyse de sang WO2010043668A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP08166899.8 2008-10-17
EP08166899 2008-10-17

Publications (1)

Publication Number Publication Date
WO2010043668A1 true WO2010043668A1 (fr) 2010-04-22

Family

ID=40524807

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/EP2009/063470 WO2010043668A1 (fr) 2008-10-17 2009-10-15 Points de sang séché pour une analyse de sang

Country Status (1)

Country Link
WO (1) WO2010043668A1 (fr)

Cited By (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2012028184A1 (fr) * 2010-09-01 2012-03-08 Zentech S.A. Analyse d'échantillons de sang provenant de gouttes de sang séché
WO2013044124A1 (fr) 2011-09-23 2013-03-28 Nanoink, Inc. Analyse quantitative précise de biomarqueurs dans des échantillons
US20140087963A1 (en) * 2012-08-29 2014-03-27 Arizona Board of Regents, a body Corporate of the State of Arizona, Acting for and on Behalf of Ariz Immunosignaturing: a path to early diagnosis and health monitoring
JP2015507211A (ja) * 2012-02-14 2015-03-05 ウオーターズ・テクノロジーズ・コーポレイシヨン 溶解可能なサンプル収集領域を有する乾燥サンプル担持体
US9321095B2 (en) 2010-06-30 2016-04-26 General Electric Company Apparatuses and methods for cutting porous substrates
US11371990B2 (en) 2016-11-11 2022-06-28 Cowper Sciences Inc. Methods for identifying candidate biomarkers
US11747334B2 (en) 2016-06-20 2023-09-05 Cowper Sciences Inc. Methods for differential diagnosis of autoimmune diseases
US11774446B2 (en) 2016-06-20 2023-10-03 Cowper Sciences Inc. Methods for diagnosis and treatment of autoimmune diseases
US11971410B2 (en) 2017-09-15 2024-04-30 Arizona Board Of Regents On Behalf Of Arizona State University Methods of classifying response to immunotherapy for cancer
US11976274B2 (en) 2019-10-02 2024-05-07 Arizona Board Of Regents On Behalf Of Arizona State University Methods and compositions for identifying neoantigens for use in treating and preventing cancer

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0583078A2 (fr) * 1992-07-14 1994-02-16 Wallac Oy Appareil et méthode de manipulation d'échantillons
US5432097A (en) * 1993-11-09 1995-07-11 Yourno; Joseph Method for recovery of blood cells from dried blood spots on filter paper
WO1997047764A1 (fr) * 1996-06-11 1997-12-18 Valtion Teknillinen Tutkimuskeskus Methode pour analyser des echantillons de matrice glucidique
US20050158814A1 (en) * 2002-04-29 2005-07-21 Aerts Johannes Maria Franciscus G. Means and methods for detecting endoglycosidase activity
EP1939604A1 (fr) * 2006-12-29 2008-07-02 Preanalytix GmbH Dispositif de collecte pour le déblocage sélectif d'un échantillon biologique

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0583078A2 (fr) * 1992-07-14 1994-02-16 Wallac Oy Appareil et méthode de manipulation d'échantillons
US5432097A (en) * 1993-11-09 1995-07-11 Yourno; Joseph Method for recovery of blood cells from dried blood spots on filter paper
WO1997047764A1 (fr) * 1996-06-11 1997-12-18 Valtion Teknillinen Tutkimuskeskus Methode pour analyser des echantillons de matrice glucidique
US20050158814A1 (en) * 2002-04-29 2005-07-21 Aerts Johannes Maria Franciscus G. Means and methods for detecting endoglycosidase activity
EP1939604A1 (fr) * 2006-12-29 2008-07-02 Preanalytix GmbH Dispositif de collecte pour le déblocage sélectif d'un échantillon biologique

Non-Patent Citations (5)

* Cited by examiner, † Cited by third party
Title
BERGQVIST Y ET AL: "Improved method for the simultaneous determination of proguanil and its metabolites by high-performance liquid chromatography and solid-phase extraction of 100-mul capillary blood samples dried on sampling paper", JOURNAL OF CHROMATOGRAPHY B: BIOMEDICAL SCIENCES & APPLICATIONS, ELSEVIER, AMSTERDAM, NL, vol. 719, no. 1-2, 20 November 1998 (1998-11-20), pages 141 - 149, XP004144822, ISSN: 1570-0232 *
ERHARDT J G ET AL: "Rapid and simple measurement of retinol in human dried whole blood spots", JOURNAL OF NUTRITION, WISTAR INSTITUTE OF ANATOMY AND BIOLOGY, PHILADELPHIA, PA, US, vol. 132, no. 2, 1 February 2002 (2002-02-01), pages 318 - 321, XP002258787, ISSN: 0022-3166 *
IRWIN D C ET AL: "Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects", BIOTECHNOLOGY AND BIOENGINEERING, vol. 42, no. 8, November 1993 (1993-11-01), pages 1002 - 1013, XP002523929 *
MAGLIONE GIUSEPPE ET AL: "Properties of a genetically reconstructed Prevotella ruminicola endoglucanase", APPLIED AND ENVIRONMENTAL MICROBIOLOGY, vol. 58, no. 11, November 1992 (1992-11-01), pages 3593 - 3597, XP002090937, ISSN: 0099-2240 *
ZURFLUH ET AL: "Screening for tetrahydrobiopterin deficiencies using dried blood spots on filter paper", MOLECULAR GENETICS AND METABOLISM, ACADEMIC PRESS, SAN DIEGO, CA, US, vol. 86, 1 December 2005 (2005-12-01), pages 96 - 103, XP005197880, ISSN: 1096-7192 *

Cited By (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US9321095B2 (en) 2010-06-30 2016-04-26 General Electric Company Apparatuses and methods for cutting porous substrates
WO2012028184A1 (fr) * 2010-09-01 2012-03-08 Zentech S.A. Analyse d'échantillons de sang provenant de gouttes de sang séché
WO2013044124A1 (fr) 2011-09-23 2013-03-28 Nanoink, Inc. Analyse quantitative précise de biomarqueurs dans des échantillons
JP2015507211A (ja) * 2012-02-14 2015-03-05 ウオーターズ・テクノロジーズ・コーポレイシヨン 溶解可能なサンプル収集領域を有する乾燥サンプル担持体
EP2815223A4 (fr) * 2012-02-14 2015-10-28 Waters Technologies Corp Support d'échantillon séché ayant des régions de collecte d'échantillon aptes à se dissoudre
US9488551B2 (en) 2012-02-14 2016-11-08 Waters Technologies Corporation Dried sample carrier having dissolvable sample regions
US20140087963A1 (en) * 2012-08-29 2014-03-27 Arizona Board of Regents, a body Corporate of the State of Arizona, Acting for and on Behalf of Ariz Immunosignaturing: a path to early diagnosis and health monitoring
US11747334B2 (en) 2016-06-20 2023-09-05 Cowper Sciences Inc. Methods for differential diagnosis of autoimmune diseases
US11774446B2 (en) 2016-06-20 2023-10-03 Cowper Sciences Inc. Methods for diagnosis and treatment of autoimmune diseases
US11371990B2 (en) 2016-11-11 2022-06-28 Cowper Sciences Inc. Methods for identifying candidate biomarkers
US11971410B2 (en) 2017-09-15 2024-04-30 Arizona Board Of Regents On Behalf Of Arizona State University Methods of classifying response to immunotherapy for cancer
US11976274B2 (en) 2019-10-02 2024-05-07 Arizona Board Of Regents On Behalf Of Arizona State University Methods and compositions for identifying neoantigens for use in treating and preventing cancer

Similar Documents

Publication Publication Date Title
WO2010043668A1 (fr) Points de sang séché pour une analyse de sang
US8399186B2 (en) Simultaneous detection of metabolic enzyme activity and metabolite levels
Sasaki et al. Correlation between X‐ray diffraction measurements of cellulose crystalline structure and the susceptibility to microbial cellulase
Zheng et al. Non-ionic surfactants and non-catalytic protein treatment on enzymatic hydrolysis of pretreated creeping wild ryegrass
Lupoi et al. Evaluation of nanoparticle‐immobilized cellulase for improved ethanol yield in simultaneous saccharification and fermentation reactions
Khanahmadi et al. Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
Vasconcellos et al. Addition of metal ions to a (hemi) cellulolytic enzymatic cocktail produced in-house improves its activity, thermostability, and efficiency in the saccharification of pretreated sugarcane bagasse
Hägerdal et al. Association of β‐glucosidase with intact cells of Thermoactinomyces
BRPI0816177B1 (pt) processo para a conversão de uma matéria-prima lignocelulósica pré-tratada em açúcares solúveis
EP2285971B1 (fr) Fermentation de matière contenant de la lignocellulose
BRPI0816389B1 (pt) métodos de diminuição da quantidade de uma preparação de celulase total requerida para hidrolisar um material celulósico e de hidrólise de um material celulósico
Lopez et al. A polymer multilayer based amperometric biosensor for the detection of lactose in the presence of high concentrations of glucose
Xiong et al. Simultaneous isolation of DNA, RNA, and protein from Medicago truncatula L.
Ray et al. Phanerochaete chrysosporium produces a diverse array of extracellular enzymes when grown on sorghum
Plagemann et al. Microwave‐assisted covalent immobilization of enzymes on inorganic surfaces
de Lourdes TM Polizeli et al. Enzymes involved in the biodegradation of sugarcane biomass: challenges and perspectives
Skjærvø et al. Smart blood spots for whole blood protein analysis
Gavlighi et al. Enhanced enzymatic cellulose degradation by cellobiohydrolases via product removal
Zhai et al. Understanding the slowdown of whole slurry hydrolysis of steam pretreated lignocellulosic woody biomass catalyzed by an up-to-date enzyme cocktail
Jung et al. Effect of cellulolytic enzyme binding on lignin isolated from alkali and acid pretreated switchgrass on enzymatic hydrolysis
Hamid et al. Enzymatic hydrolysis of low temperature alkali pretreated wheat straw using immobilized β-xylanase nanoparticles
Velleste et al. Reducing end-specific fluorescence labeled celluloses for cellulase mode of action
CN114563507A (zh) 一种动物组织内的β-受体激动剂残留的处理方法、检测方法及应用
Mackenzie et al. Effects of NIPAm polymer additives on the enzymatic hydrolysis of Avicel and pretreated Miscanthus
Ariaeenejad et al. Enhancing the ethanol production by exploiting a novel metagenomic-derived bifunctional xylanase/β-glucosidase enzyme with improved β-glucosidase activity by a nanocellulose carrier

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 09744361

Country of ref document: EP

Kind code of ref document: A1

NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 09744361

Country of ref document: EP

Kind code of ref document: A1