JPS6018762A - 安定化された凝固対照試薬 - Google Patents

安定化された凝固対照試薬

Info

Publication number: JPS6018762A
Authority: JP; Japan
Prior art keywords: water; medium; reagent; plasma; group
Prior art date: 1983-06-06
Legal status (The legal status 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 status listed.): Granted

Application number

JP11322684A

Other languages

English (en)

Japanese (ja)

Other versions

JPH0511264B2 (da

Inventor

マイケル・ケビン・ホスキンズ

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Ortho Clinical Diagnostics Inc

Original Assignee

Ortho Diagnostic Systems Inc

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.)

1983-06-06

Filing date

1984-06-04

Publication date

1985-01-30

1984-06-04 Application filed by Ortho Diagnostic Systems Inc filed Critical Ortho Diagnostic Systems Inc

1985-01-30 Publication of JPS6018762A publication Critical patent/JPS6018762A/ja

1993-02-15 Publication of JPH0511264B2 publication Critical patent/JPH0511264B2/ja

Status Granted legal-status Critical Current

Links

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Landscapes

Investigating Or Analysing Biological Materials (AREA)
Compounds Of Unknown Constitution (AREA)
Agricultural Chemicals And Associated Chemicals (AREA)

JP11322684A 1983-06-06 1984-06-04 安定化された凝固対照試薬 Granted JPS6018762A (ja)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US50121683A	1983-06-06	1983-06-06
US501216		1983-06-06

Related Child Applications (1)

Application Number	Title	Priority Date	Filing Date
JP34986791A Division JPH0560753A (ja)	1983-06-06	1991-12-10	血漿レニン対照試薬

Publications (2)

Publication Number	Publication Date
JPS6018762A true JPS6018762A (ja)	1985-01-30
JPH0511264B2 JPH0511264B2 (da)	1993-02-15

Family

ID=23992589

Family Applications (2)

Application Number	Title	Priority Date	Filing Date
JP11322684A Granted JPS6018762A (ja)	1983-06-06	1984-06-04	安定化された凝固対照試薬
JP34986791A Pending JPH0560753A (ja)	1983-06-06	1991-12-10	血漿レニン対照試薬

Family Applications After (1)

Application Number	Title	Priority Date	Filing Date
JP34986791A Pending JPH0560753A (ja)	1983-06-06	1991-12-10	血漿レニン対照試薬

Country Status (6)

Country	Link
JP (2)	JPS6018762A (da)
AU (1)	AU584859B2 (da)
CA (1)	CA1226795A (da)
DK (1)	DK275384A (da)
IL (1)	IL72032A0 (da)
NO (1)	NO842260L (da)

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPH03144364A (ja) *	1989-10-30	1991-06-19	Takami Nagata	血球計数用抗凝固剤
JPH0560753A (ja) *	1983-06-06	1993-03-12	Ortho Diagnostic Syst Inc	血漿レニン対照試薬
JP2009545751A (ja) *	2006-08-04	2009-12-24	バイオ−ラッドラボラトリーズ，インコーポレイティド	血液凝固試験に関する標準／参照／対照
WO2010101206A1 (ja) *	2009-03-05	2010-09-10	株式会社ビー・エム・エル	管理試料の安定化剤、当該安定化剤を含有する管理試料、及び、当該管理試料を含む測定用キット

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1230300A (en) *	1983-06-06	1987-12-15	Michael K. Hoskins	Stabilized isoenzyme control product
CA1226794A (en) *	1983-06-06	1987-09-15	Michael K. Hoskins	Stabilized multiparameter control product
US4663295A (en) *	1983-06-29	1987-05-05	Ciba Corning Diagnostics Corp.	Estrogen-progesterone control reagents and methods for making same
WO2004046723A1 (ja) *	2002-11-18	2004-06-03	Denka Seiken Co., Ltd.	血清および血漿の測定値乖離を防止する免疫測定法

Citations (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS5191310A (da) *	1974-12-31	1976-08-10
JPS5757661A (en) *	1980-09-25	1982-04-06	Daicel Ltd	Film for separately packing sliced cheese

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1226795A (en) *	1983-06-06	1987-09-15	Michael K. Hoskins	Stabilized coagulation control products
CA1230300A (en) *	1983-06-06	1987-12-15	Michael K. Hoskins	Stabilized isoenzyme control product
CA1226794A (en) *	1983-06-06	1987-09-15	Michael K. Hoskins	Stabilized multiparameter control product
JPH0511264A (ja) *	1991-07-05	1993-01-19	Hitachi Ltd	液晶表示装置

1984
- 1984-05-25 CA CA000455086A patent/CA1226795A/en not_active Expired
- 1984-06-04 DK DK275384A patent/DK275384A/da not_active Application Discontinuation
- 1984-06-04 JP JP11322684A patent/JPS6018762A/ja active Granted
- 1984-06-05 IL IL72032A patent/IL72032A0/xx unknown
- 1984-06-05 AU AU29086/84A patent/AU584859B2/en not_active Ceased
- 1984-06-05 NO NO842260A patent/NO842260L/no unknown
1991
- 1991-12-10 JP JP34986791A patent/JPH0560753A/ja active Pending

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS5191310A (da) *	1974-12-31	1976-08-10
JPS5757661A (en) *	1980-09-25	1982-04-06	Daicel Ltd	Film for separately packing sliced cheese

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPH0560753A (ja) *	1983-06-06	1993-03-12	Ortho Diagnostic Syst Inc	血漿レニン対照試薬
JPH03144364A (ja) *	1989-10-30	1991-06-19	Takami Nagata	血球計数用抗凝固剤
JP2009545751A (ja) *	2006-08-04	2009-12-24	バイオ−ラッドラボラトリーズ，インコーポレイティド	血液凝固試験に関する標準／参照／対照
WO2010101206A1 (ja) *	2009-03-05	2010-09-10	株式会社ビー・エム・エル	管理試料の安定化剤、当該安定化剤を含有する管理試料、及び、当該管理試料を含む測定用キット
US8623654B2 (en)	2009-03-05	2014-01-07	Bml, Inc.	Stabilizing agent for control material, control material containing the stabilizing agent, and measurement kit comprising the control material
JP5425062B2 (ja) *	2009-03-05	2014-02-26	株式会社ビー・エム・エル	Ｄ−マンニトールを含有する管理試料を用いるグリコアルブミン等の測定方法

Also Published As

Publication number	Publication date
AU584859B2 (en)	1989-06-08
IL72032A0 (en)	1984-10-31
DK275384D0 (da)	1984-06-04
DK275384A (da)	1984-12-07
JPH0560753A (ja)	1993-03-12
JPH0511264B2 (da)	1993-02-15
CA1226795A (en)	1987-09-15
NO842260L (no)	1984-12-07
AU2908684A (en)	1984-12-13

Publication	Publication Date	Title
Astrup et al.	1959	Thromboplastic and fibrinolytic activity of the human aorta
Al-Mondhiry et al.	1975	Fibrinogen"" New York"--an abnormal fibrinogen associated with thromboembolism: functional evaluation
JP3055933B2 (ja)	2000-06-26	改良された安定な凝固対照
JPH05207897A (ja)	1993-08-20	トロンボプラスチン抽出物、試薬およびそれらの調製方法
Hedner	1973	Studies on an inhibitor of plasminogen activation in human serum
Kirschstein et al.	1989	Impaired fibrinolytic capacity and tissue plasminogen activator release in patients with restenosis after percutaneous transluminal coronary angioplasty (PTCA)
Sise et al.	1955	Plasma Thromboplastin Component (PTC) Deficiency Produced by Prolonged Administration of Prothrombopenic Anticoagulants.
EP0155852B1 (en)	1990-05-02	Thrombin-binding substance and process for its production
JPS6018762A (ja)	1985-01-30	安定化された凝固対照試薬
Lacombe et al.	1975	A hitherto undescribed plasma factor acting at the contact phase of blood coagulation (Flaujeac factor): case report and coagulation studies
Bithell et al.	1970	Variant of factor IX deficiency in female with 45, X Turner’s syndrome
Francis et al.	1984	Demonstration of in situ fibrin degradation in pathologic thrombi
DIDISHEIM	1962	Hageman factor deficiency (Hageman trait): case report and review of the literature
Fruchtman et al.	1986	Disseminated intravascular coagulation
Newland et al.	1991	Elevated plasminogen activator inhibitor levels found in patients with malignant conditions
US3228841A (en)	1966-01-11	Diagnostic reagent composition for determining blood coagulation factors and method of use
Almasio et al.	1986	Characterization of the molecular forms of fibronectin in fulminant hepatic failure
De Stefano et al.	1990	Mesenteric vein thrombosis in protein S congenital deficiency
Eng et al.	2000	Soluble thrombomodulin antigen as a marker for endothelial damage during liver transplantation
Bick	2019	Hereditary plasma protein disorders
Merskey	1982	DIC: Identification and management
Ende et al.	1964	Activation of a fibrinolytic system in a dog with mast cell tumor
Baker et al.	1960	Some properties of platelet cofactor I concentrates of bovine origin
JPH06130066A (ja)	1994-05-13	Ｔａｔの安定化方法およびｔａｔ測定キット用標準物質
Flute	1964	Haemorrhage and fibrinolysis