نتایج جستجو برای: coagulation factor ix

تعداد نتایج: 893342  

Journal: :medical journal of islamic republic of iran 0
kamran mousavi hosseini blood transfusion research center, high institute for research and education in transfusion medicine, tehran, iran.سازمان اصلی تایید شده: سازمان انتقال خون ایران (blood transfusion research center)سازمان های دیگر: blood transfusion research center, saleh nasiri blood transfusion research center, high institute for research and education in transfusion medicine, tehran, iran.سازمان اصلی تایید شده: سازمان انتقال خون ایران (blood transfusion research center)سازمان های دیگر: blood transfusion research center,

background: factor vii concentrates are used in patients with congenital or acquired factor vii deficiency or treatment of hemophilia patients with inhibitors. in this research, immunoaffinity chromatography was used to purify factor vii from prothrombin complex (prothrombin-proconvertin-stuart factor-antihemophilic factor b or ppsb) which contains coagulation factors ii, vii, ix and x. the aim...

Journal: :Chemical communications 2014
Y Daijima T Komatsu

We describe the synthesis of a haemoglobin (Hb) wrapped covalently by recombinant human serum albumin mutants [HSA(Y161H)] containing Mn(III) protoporphyrin IX (MnPP), the Hb-[HSA(Y161H)-MnPP]3 cluster, highlighting the formation of its O2-complex stable even in H2O2 solution.

2011
CSL Behring

only DESCRIPTION Coagulation Factor IX (Human), Mononine, is a sterile, stable, lyophilized concentrate of Factor IX prepared from pooled human plasma and is intended for use in therapy of Factor IX deficiency, known as Hemophilia B or Christmas disease. Mononine is purified of extraneous plasma-derived proteins, including Factors II, VII and X, by use of immunoaffinity chromatography. A murine...

2012
N. A. Orlova S. V. Kovnir I. I. Vorobiev A.G. Gabibov

Factor IX is a zymogen enzyme of the blood coagulation cascade. Inherited absence or deficit of the IX functional factor causes bleeding disorder hemophilia B, which requires constant protein replacement therapy. Reviewed herein are the current state in the manufacturing of FIX, improved variants of the recombinant protein for therapy, transgenic organisms for obtaining FIX, and the advances in...

Journal: :Blood 2009
Dmitri V Kravtsov Anton Matafonov Erik I Tucker Mao-Fu Sun Peter N Walsh Andras Gruber David Gailani

During surface-initiated blood coagulation in vitro, activated factor XII (fXIIa) converts factor XI (fXI) to fXIa. Whereas fXI deficiency is associated with a hemorrhagic disorder, factor XII deficiency is not, suggesting that fXI can be activated by other mechanisms in vivo. Thrombin activates fXI, and several studies suggest that fXI promotes coagulation independent of fXII. However, a recen...

Journal: :The Journal of biological chemistry 2004
Mingdong Huang Barbara C Furie Bruce Furie

The binding of Factor IX to membranes during blood coagulation is mediated by the N-terminal gamma-carboxyglutamic acid-rich (Gla) domain, a membrane-anchoring domain found on vitamin K-dependent blood coagulation and regulatory proteins. Conformation-specific anti-Factor IX antibodies are directed at the calcium-stabilized Gla domain and interfere with Factor IX-membrane interaction. One such ...

Journal: :Blood 1996
G J Broze D A Higuchi

Coagulation is initiated by the binding of factor VIIa to tissue factor, with resultant limited factor IX and X activation and thrombin production. Owing to the feedback inhibition of the factor VIIa/tissue factor complex by tissue factor pathway inhibitor (TFPI), additional factor X activation and thrombin generation must proceed through a pathway involving factors VIII, IX, and XI. Experiment...

2009
Dmitri V. Kravtsov Anton Matafonov Erik I. Tucker Mao-fu Sun Peter N. Walsh Andras Gruber David Gailani

During surface-initiated blood coagulation in vitro, activated factor XII (fXIIa) converts factor XI (fXI) to fXIa. Whereas fXI deficiency is associated with a hemorrhagic disorder, factor XII deficiency is not, suggesting that fXI can be activated by other mechanisms in vivo. Thrombin activates fXI, and several studies suggest that fXI promotes coagulation independent of fXII. However, a recen...

Edward Graham Tuddenham, Manijeh Lak, Morteza Karimipour, Nafiseh Nafissi, Peter Green, Sirous Zeinali,

Background: Heterogeneous mutations in the human coagulation factor IX gene lead to an X-linked recessive bleeding disorder known as hemophilia B. The disease is distributed worldwide with no ethnic or geographical priority. Materials and Methods: The aim of this study was to characterize the factor IX gene mutations in 28 unrelated Iranian hemophilia B patients. Polymerase chain reaction (PCR)...

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