OA11745A - Method and kit for extracting prion protein. Method and kit for extracting prion protein. - Google Patents

Method and kit for extracting prion protein. Method and kit for extracting prion protein. Download PDF

Info

Publication number: OA11745A
Authority: OA; OAPI
Prior art keywords: prion protein; aqueous; abnormal; lyotropic; préparation
Prior art date: 1999-01-08

Application number

OA1200100178A

Other languages

English (en)

Inventor

Andrew J Alpert

Mary Jo Schmerr

Original Assignee

Andrew J Alpert

Us Agriculture

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.)

1999-01-08

Filing date

2000-01-07

Publication date

2005-05-13

2000-01-07 Application filed by Andrew J Alpert, Us Agriculture filed Critical Andrew J Alpert

2005-05-13 Publication of OA11745A publication Critical patent/OA11745A/en

Links

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210000000952 spleen Anatomy 0.000 description 1
229910001220 stainless steel Inorganic materials 0.000 description 1
239000010935 stainless steel Substances 0.000 description 1
239000000758 substrate Substances 0.000 description 1
239000004094 surface-active agent Substances 0.000 description 1
210000004243 sweat Anatomy 0.000 description 1
230000009897 systematic effect Effects 0.000 description 1
210000001138 tear Anatomy 0.000 description 1
YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 1
210000001541 thymus gland Anatomy 0.000 description 1
238000002054 transplantation Methods 0.000 description 1
239000003656 tris buffered saline Substances 0.000 description 1
210000002700 urine Anatomy 0.000 description 1
238000005406 washing Methods 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/962—Prevention or removal of interfering materials or reactants or other treatment to enhance results, e.g. determining or preventing nonspecific binding

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Gastroenterology & Hepatology (AREA)
Zoology (AREA)
Toxicology (AREA)
Analytical Chemistry (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

OA1200100178A 1999-01-08 2000-01-07 Method and kit for extracting prion protein. Method and kit for extracting prion protein. OA11745A (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US11527299P	1999-01-08	1999-01-08
US09/420,850 US6150172A (en)	1999-01-08	1999-10-19	Method and kit for extracting prion protein

Publications (1)

Publication Number	Publication Date
OA11745A true OA11745A (en)	2005-05-13

Family

ID=26813023

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
OA1200100178A OA11745A (en)	1999-01-08	2000-01-07	Method and kit for extracting prion protein. Method and kit for extracting prion protein.

Country Status (23)

Country	Link
US (1)	US6150172A (id)
EP (1)	EP1147415A4 (id)
JP (1)	JP2002534681A (id)
KR (1)	KR20010089776A (id)
CN (1)	CN1135235C (id)
AU (1)	AU761319B2 (id)
BR (1)	BR0007274A (id)
CA (1)	CA2358285A1 (id)
CZ (1)	CZ20012469A3 (id)
EA (1)	EA004953B1 (id)
EE (1)	EE200100358A (id)
GE (1)	GEP20033036B (id)
HK (1)	HK1044588B (id)
HU (1)	HUP0104890A3 (id)
ID (1)	ID29442A (id)
IL (1)	IL143974A0 (id)
NO (1)	NO20013193L (id)
NZ (1)	NZ513215A (id)
OA (1)	OA11745A (id)
PL (1)	PL349132A1 (id)
SK (1)	SK9492001A3 (id)
TR (1)	TR200101935T2 (id)
WO (1)	WO2000040966A1 (id)

Families Citing this family (46)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6972177B1 (en)	1996-04-03	2005-12-06	Stichting Instituut Voor Dierhouderij En Diergezondheid	Method for the detection of prion diseases
US6322802B1 (en)	1999-06-01	2001-11-27	The Regents Of The University Of California	Method of sterilizing
US6719988B2 (en)	1997-02-21	2004-04-13	The Regents Of The University Of California	Antiseptic compositions for inactivating prions
US20060008494A1 (en) *	1997-02-21	2006-01-12	The Regents Of The University Of California	Complete inactivation of infectious proteins
US6331296B1 (en)	1999-06-01	2001-12-18	Stanley B. Prusiner	Food additives which affect conformationally altered proteins
US6720355B2 (en) *	1997-02-21	2004-04-13	The Regents Of The University Of California	Sodium dodecyl sulfate compositions for inactivating prions
FR2774988B1 (fr) *	1998-02-16	2000-05-05	Commissariat Energie Atomique	Procede de purification de la prpres a partir d'un echantillon biologique et ses applications
GB9902659D0 (en) *	1999-02-05	1999-03-31	Microbiological Res Authority	Assay with reduced background
CA2364686C (en)	1999-02-11	2007-04-24	Id-Lelystad, Instituut Voor Dierhouderij En Diergezondheid B.V.	Prion test
US6605445B1 (en) *	1999-02-22	2003-08-12	Bayer Corporation	Rapid method of determining clearance of prion protein
US7041807B1 (en)	1999-06-23	2006-05-09	Caprion Pharmaceuticals, Inc.	Antibodies to a YYX epitope of a mammalian prion protein
US6437102B1 (en) *	1999-11-24	2002-08-20	Bayer Corporation	Method of separating prions from biological materials
US20030050276A1 (en) *	2001-08-15	2003-03-13	Cunanan Crystal M.	Treatment of tissue, instruments and work surfaces to remove infectious agents
IES20010042A2 (en) *	2001-01-19	2002-12-11	Enfer Technology Ltd	Test for transmissible spongiform encephalopathies
US20020192731A1 (en) *	2001-04-12	2002-12-19	H. Shih Jason C.	Method and composition for sterilizing surgical instruments
US8414774B2 (en) *	2001-04-25	2013-04-09	Agilent Technologies, Inc.	Systems and methods for high-throughput screening of fluidic samples
US20050123970A1 (en) *	2001-04-25	2005-06-09	Can Ozbal	High throughput autosampler
WO2002093168A1 (en) *	2001-05-15	2002-11-21	Gradipore Limited	Prion diagnostic test
FR2827047B1 (fr) *	2001-07-03	2003-09-26	Apoh Technollgies Sa	Procede de separation et/ou detection et/ou identification et/ou quantification de proteines prions
US6591991B2 (en) *	2001-08-06	2003-07-15	Luce Belle	Collapsible tire stand
US7045297B2 (en) *	2001-11-14	2006-05-16	Prion Developmental Laboratories, Inc.	Rapid prion-detection assay
US20030092090A1 (en) *	2001-11-14	2003-05-15	Kiamars Hajizadeh	Rapid prion-detection device, system, and test kit
BRPI0307976B8 (pt) †	2002-02-28	2021-07-27	Microsens Biophage Ltd	processo para a ligação seletiva de uma forma anormal agregativa de uma proteína, e, processo ou ensaio quanto à presença de uma forma agregativa anormal de uma proteína de uma amostra
AU2003280457A1 (en) *	2002-06-27	2004-01-19	University Of Marlyland, Baltimore	Methods for detecting and inactivating a prion
DE10230141B4 (de) *	2002-07-04	2004-07-15	Priontype Gmbh	Verfahren und Kit zur Anreicherung und zum Nachweis von veränderten Prion-Proteinen (PrPSc)
US20040018120A1 (en) *	2002-07-29	2004-01-29	Craig Rappin	Sample preparation device and method
US20040018575A1 (en) *	2002-07-29	2004-01-29	Craig Rappin	Sample preparation device and method
CH693953A5 (de) *	2002-10-15	2004-05-14	Tecan Trading Ag	Verfahren zum Anreichern von Proteinloesungen durch hydrophile Wechselwirkungschromatographie (HILIC) und Verduennungsloesung fuer proteinhaltige Fluessigkeiten.
US20040175775A1 (en) *	2002-11-08	2004-09-09	Neil Cashman	Method of detecting PrPsc in eye fluid
AU2003296953A1 (en) *	2002-12-12	2004-07-09	Strategic Diagnostics Inc.	Compositions and methods for detecting animal by product in feed
FR2849205B1 (fr) *	2002-12-20	2005-02-11	Afssa	Procede d'amplification de la detection de la prpsc et utilisation d'un ligand adjuvant macrocyclique pour une telle amplification
US20090068640A1 (en) *	2003-06-27	2009-03-12	Robert Rohwer	Methods for detecting and inactivating a prion
US20050054003A1 (en) *	2003-09-10	2005-03-10	Stenland Christopher J.	Prion clearance using particulate metal oxides
DE10354207B8 (de) *	2003-11-20	2006-06-14	Priontype Gmbh & Co.Kg	Verfahren zum Nachweis von pathologisch veränderten Prion-Proteinen (PrPSc) und Kit zur Durchführung des Verfahrens
JP4724816B2 (ja) *	2005-09-06	2011-07-13	シャープ株式会社	タンパク質の測定方法
DE102006044795A1 (de) *	2006-09-13	2008-03-27	Schweigert, Florian, Prof. Dr.med.vet.	Bestimmung von Inhaltsstoffen aus biologischen Materialien
CN101820966B (zh) *	2007-06-04	2017-10-27	高压生物科学公司	分子的压力提高的提取和分配
JP5433580B2 (ja) *	2007-11-02	2014-03-05	バイオシアスライフサイエンシーズ，インコーポレイテッド	試料注入システム
US20120156794A1 (en) *	2008-03-19	2012-06-21	Florian Schweigert	Method for the extraction and detection of fat-soluble components from biological materials
US20090286301A1 (en) *	2008-05-07	2009-11-19	Pressure Biosciences Inc.	Extraction of biomolecular complexes assisted by alternating hydrostatic pressure
RS59896B1 (sr) *	2009-04-15	2020-03-31	Abraxis Bioscience Llc	Kompozicije nanočestica bez priona i postupci povezani sa njima
CN103255142B (zh) *	2012-02-21	2017-07-25	上海转基因研究中心	一种利用RNAi调控内源性朊蛋白表达的方法及其应用
CN102757493A (zh) *	2012-07-11	2012-10-31	北京健翔和牧生物科技有限公司	一种制备鸡痘病毒抗体的方法
WO2019087393A1 (en) *	2017-11-06	2019-05-09	Shimadzu Corporation	Component separation method using supercritical fluid chromatograph
US11808675B2 (en) *	2019-06-13	2023-11-07	Agilent Technologies, Inc.	Room temperature methods for preparing biological analytes
EP4056175A4 (en) *	2019-11-08	2023-12-06	Central Glass Company, Limited	METHOD FOR SELECTIVELY KILLING CELLS CONTAINING PROTEIN AGGREGATES, RELATED KIT, THERAPEUTIC DRUG FOR PROTEIN MISFOLDING DISEASES, AND DRUG PRODUCT FOR REMOVING PROTEIN AGGREGATES FROM BLOOD PRODUCT

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6020537A (en) *	1994-05-13	2000-02-01	The Regents Of The University Of California	Prion protein standard and method of making same
US5998149A (en) *	1996-04-05	1999-12-07	The United States Of America As Represented By The Department Of Health And Human Services	Method of detecting transmissible spongiform encephalopathies
US5808011A (en) *	1996-07-01	1998-09-15	Biopure Corporation	Method for chromatographic removal of prions

1999
- 1999-10-19 US US09/420,850 patent/US6150172A/en not_active Expired - Fee Related
2000
- 2000-01-07 KR KR1020017008560A patent/KR20010089776A/ko not_active Withdrawn
- 2000-01-07 EP EP00904258A patent/EP1147415A4/en not_active Withdrawn
- 2000-01-07 ID IDW00200101710A patent/ID29442A/id unknown
- 2000-01-07 EA EA200100756A patent/EA004953B1/ru not_active IP Right Cessation
- 2000-01-07 BR BR0007274-5A patent/BR0007274A/pt not_active IP Right Cessation
- 2000-01-07 TR TR2001/01935T patent/TR200101935T2/xx unknown
- 2000-01-07 PL PL00349132A patent/PL349132A1/xx not_active Application Discontinuation
- 2000-01-07 WO PCT/US2000/000457 patent/WO2000040966A1/en not_active Ceased
- 2000-01-07 CA CA002358285A patent/CA2358285A1/en not_active Abandoned
- 2000-01-07 HU HU0104890A patent/HUP0104890A3/hu unknown
- 2000-01-07 CN CNB008044058A patent/CN1135235C/zh not_active Expired - Fee Related
- 2000-01-07 GE GEAP20006037A patent/GEP20033036B/en unknown
- 2000-01-07 SK SK949-2001A patent/SK9492001A3/sk unknown
- 2000-01-07 IL IL14397400A patent/IL143974A0/xx unknown
- 2000-01-07 CZ CZ20012469A patent/CZ20012469A3/cs unknown
- 2000-01-07 NZ NZ513215A patent/NZ513215A/xx unknown
- 2000-01-07 OA OA1200100178A patent/OA11745A/en unknown
- 2000-01-07 AU AU26043/00A patent/AU761319B2/en not_active Ceased
- 2000-01-07 HK HK02106255.5A patent/HK1044588B/zh not_active IP Right Cessation
- 2000-01-07 EE EEP200100358A patent/EE200100358A/xx unknown
- 2000-01-07 JP JP2000592634A patent/JP2002534681A/ja active Pending
2001
- 2001-06-25 NO NO20013193A patent/NO20013193L/no not_active Application Discontinuation

Also Published As

Publication number	Publication date
HK1044588B (zh)	2004-12-03
CA2358285A1 (en)	2000-07-13
BR0007274A (pt)	2001-10-30
HUP0104890A2 (hu)	2002-04-29
US6150172A (en)	2000-11-21
EE200100358A (et)	2002-12-16
SK9492001A3 (en)	2002-06-04
ID29442A (id)	2001-08-30
NO20013193D0 (no)	2001-06-25
WO2000040966A1 (en)	2000-07-13
CN1342266A (zh)	2002-03-27
EP1147415A1 (en)	2001-10-24
EP1147415A4 (en)	2004-06-30
CN1135235C (zh)	2004-01-21
AU2604300A (en)	2000-07-24
IL143974A0 (en)	2002-04-21
TR200101935T2 (tr)	2002-01-21
EA200100756A1 (ru)	2001-12-24
EA004953B1 (ru)	2004-10-28
HUP0104890A3 (en)	2003-09-29
KR20010089776A (ko)	2001-10-08
NZ513215A (en)	2002-12-20
CZ20012469A3 (cs)	2002-02-13
NO20013193L (no)	2001-08-15
PL349132A1 (en)	2002-07-01
HK1044588A1 (en)	2002-10-25
JP2002534681A (ja)	2002-10-15
AU761319B2 (en)	2003-06-05
GEP20033036B (en)	2003-07-25

Publication	Publication Date	Title
US6150172A (en)	2000-11-21	Method and kit for extracting prion protein
Schmerr et al.	1999	Use of capillary electrophoresis and fluorescent labeled peptides to detect the abnormal prion protein in the blood of animals that are infected with a transmissible spongiform encephalopathy
JP4842478B2 (ja)	2011-12-21	生物学的試料における非通常伝達因子株によって引起こされる亜急性伝達性海綿状脳症の診断方法
Thomas et al.	1990	Synaptophysin binds to physophilin, a putative synaptic plasma membrane protein.
EP3031823B1 (en)	2018-12-19	Method of diagnosing neurodegenerative disease
US7462489B2 (en)	2008-12-09	Methods for identifying and analyzing biomarkers from plasma-derived microparticles
KR20040032826A (ko)	2004-04-17	단백질 프로파일링에 의한 신장 질병 검출 방법
ES2270582T3 (es)	2007-04-01	Procedimiento de purificacion de prpres a partir de una muestra biologica y sus aplicaciones.
EP0124896B1 (de)	1990-01-31	Verfahren zur Gewinnung von Viren bzw. Virusantigenen und deren Anwendung in Diagnose und Therapie (Impfstoff)
Schmerr et al.	1998	Capillary isoelectric focusing of the scrapie prion protein
Schmerr et al.	2000	Method and kit for extracting prion protein
ZA200105304B (en)	2001-12-13	Method and kit for extracting prion protein.
Singh et al.	1969	Identification of a protein fraction in the occipital cortex of the monkey rapidly labelled during the exposure of the animal to rhythmically flickering light
EP0558747B1 (en)	1998-01-07	Immunosorbent for diagnosis of epilepsy and group of risk
US6605445B1 (en)	2003-08-12	Rapid method of determining clearance of prion protein
MXPA01006875A (en)	2003-11-07	Method and kit for extracting prion protein
BG64291B1 (bg)	2004-08-31	М...'од и ки' за ...к''рахиран... на прион про'...ин
Williams et al.	1984	Characterization of rabbit neutrophil membrane proteins. A 140K major membrane protein is the predominant con A-binding protein
KR20230148118A (ko)	2023-10-24	생체 시료 내 지질 연관 단백질의 질량 분석을 위한 지질 연관 단백질의 정제 및 농축 방법
Kudinova et al.	1997	Isolation and characterization of soluble β-amyloid and apolipoproteins from cerebrospinal fluid
Sydow	1989	Sialic acid content in serum IgG from patients with myotonic dystrophy compared with healthy controls
Spinos	1977	Antibodies to milk antigens in human coronary heart disease
ZA200309593B (en)	2004-12-10	Method for kidney disease detection by protein profiling.