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Friday, October 16, 2020 | History

2 edition of study of the specificity of Bovine activated factor X. found in the catalog.

study of the specificity of Bovine activated factor X.

John David Lonsdale-Eccles

study of the specificity of Bovine activated factor X.

by John David Lonsdale-Eccles

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Published .
Written in English


Edition Notes

Thesis(Ph. D.)--The Queen"s University of Belfast, 1974.

The Physical Object
Pagination1 v
ID Numbers
Open LibraryOL19184126M

Factor X, also known by the eponym Stuart–Prower factor, is an enzyme (EC ) of the coagulation is a serine endopeptidase (protease group S1, PA clan).Factor X is synthesized in the liver and requires vitamin K for its synthesis.. Factor X is activated, by hydrolysis, into factor Xa by both factor IX (with its cofactor, factor VIII in a complex known as intrinsic Tenase.   Development of antibodies to thrombin and factor V with recurrent bleeding in a patient exposed to topical bovine thrombin. Blood ; Rapaport SI, Zivelin A, Minow RA, et al. Clinical significance of antibodies to bovine and human thrombin and factor V after surgical use of bovine thrombin.

The elucidation of the mechanisms of preadipocyte differentiation and fat accumulation in adipocytes is a major work in beef cattle breeding. As important post-transcriptional regulators, microRNAs (miRNAs) take part in cell proliferation, differentiation, apoptosis, and fat metabolism through binding seed sites of targeting mRNAs. The aim of this study was to isolate and identify bovine. Neudesin neurotrophic factor (NENF) is a secreted protein that is essential in multiple biological processes, including neural functions, adipogenesis, and tumorigenesis. In our previous study, NENF was significantly inhibited in the bovine adipocytes-myoblasts co-culture system. However, studies on NENF regulation of bovine muscle development and involvement in the cross-talk between adipose.

Chimeras having both the thrombin-sensitive region (TSR) and the first epidermal-growth-factor-(EGF)-like module of bovine origin expressed APC-cofactor activity similar to that of bovine protein S. Those chimeras, in which TSR or EGF1 derived from different species, manifested APC-cofactor activity similar to that of human protein S, i.e. they. Coronaviruses are RNA viruses that cause significant disease within many species, including cattle. Bovine coronavirus (BCoV) infects cattle and wild ruminants, both as a respiratory and enteric pathogen, and possesses a significant economic threat to the cattle industry. Transcription factors are proteins that activate or inhibit transcription through DNA binding and have become new targets.


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Study of the specificity of Bovine activated factor X by John David Lonsdale-Eccles Download PDF EPUB FB2

A Study of the Specificity of Bovine Activated Factor X. Author: Lonsdale-Eccles, J. The activation of bovine Factor X by bovine Factor Xa.

Archives of Biochemistry and Biophysics(1), DOI: /(82) Koen Mertens, Marijke Wortelboer, Gerbrand Van Dieijen, Rogier M. by:   Factor X and activated Factor X wcrc clutcd in separate experiments were markedly dissimilar (Fig.

Factor X yielded a single major peak of radio- activity. Activated Factor X yielded two peaks; one was associated with the excluded volume (activation Fragment L) while the other was retarded in the column (acti- vation peptide).Cited by:   Bovine Factor X was prepared from fresh blood by the method of Esnouf et al.

[17]. The combined pools of Factor X~ and X2 were activated by the coagulant fraction of Russell's viper venom [18] and purified on DEAE- Sephadex [17].Cited by: 5. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS Vol. No. 1, Janu pp.The Inhibition of Activated Bovine Coagulation Factors X and VII by Antithrombin III JOLYON JESTY Department of Medicine, State University of New York, Stony Brook, New York Received J ; revised September 6, The inhibition of activated bovine Factors VII and X by antithrombin III has been studied Cited by: The kinetic parameters of bovine factor X activation by bovine factor IXa have been determined in the absence and presence of Ca2+, thrombin-activated bovine factor VIII (VIIIa), and phospholipid.

In the present study, we have isolated from the soluble fraction of liver homogenates a potent inhibitor that competitively blocks activated factor X. Our present data suggest, therefore, that at least one mechanism by which activated factor X is removed from the circulation is intrahepatic binding of the procoagulant.

Summary. The exterase activity of bovine Factor Xa on the synthetic substrate α-N-benzoyl-L-arginine ethyl ester was used to follow the activation of Factor X by the intrinsic pathway of coagulation.

Factor IXa alone activated Factor X in a calcium-dependent reaction. 1. Thromb Res. May 1;22(3) Regulation of bovine activated protein C by protein S: the role of the cofactor protein in species specificity.

The APTT is so named because the partial thromboplastin reagent used in the test contains activators such as Kaolin or Silica to activate the contact factors in the intrinsic pathway. Calcium chloride (CaCl2) is the second reagent used in the test and is added to supply the ionized calcium required to activate prothrombin in the common pathway.

Regulation of bovine activated protein C by protein S: the role of the cofactor protein in species specificity. Thromb Res. May 1; 22 (3)– Nesheim ME, Canfield WM, Kisiel W, Mann KG. Studies of the capacity of factor Xa to protect factor Va from inactivation by activated protein C.

J Biol Chem. Feb 10; (3)– Primary Structure and Specificity of a New Member of Galectin Family from the Amethyst Deceiver Mushroom Laccaria amethystina. erythro -β-hydroxyaspartic acid in bovine factor IX and factor X. FEBS Letters(1), APPROACHES TO THE STUDY OF PROTHROMBIN CONFORMATION AND ACTIVATION IN BIOLOGICAL FLUIDS*.

BT was lyophilized from a solution containing sodium chloride and Tris-HCl, with a pH of and activated with bovine brain thromboplastin. The specific activity of BT was 40 to NIH units/mg.

BSA (fraction V, cold alcohol isolation) was purchased from Sangon Biotech Co. (catalog number: –46–8). Bovine factor X 1 (Stuart factor).

Mechanism of activation by protein from Russell's viper venom. Biochemistry. Dec 19; 11 (26)– Fujikawa K, Legaz ME, Kato H, Davie EW. The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent).

Biochemistry. Characterization of two glycoprotein variants of bovine factor X and demonstration that the factor X zymogen contains two polypeptide chains Conformation-specific antibodies: approach to the study of the vitamin K-dependent blood coagulation proteins.

Physicochemical and immunological properties of canine factor X and activated factor X. The binding of bovine Factor V, isolated Factor Va, and isolated activation intermediates to single bilayer phospholipid vesicles was studied by light scattering.

Isolation and characterization of bovine factor VII. Biochemistry14 (22), DOI: /bia Kazuo Fujikawa, Mark E. Legaz, Hisao Kato, and Earl W. Davie. Mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa(activated plasma thromboplastin antecedent).

The activated mammalian CAPN-structures, the CAPN/CAST complex in particular, have become an invaluable target model using the structure-based virtual screening of drug candidates from the discovery phase to development for over-activated CAPN linked to several diseases, such as post-ischemic injury and cataract formation.

The effect of Ca2+-binding to the enzyme is thought to include. Here we demonstrate that activated CD8(+) T-cells of HIVseropositive individuals modify serum bovine antithrombin III into an HIV-1 inhibitory factor capable of suppressing the replication of.

Activation of bovine factor IX (Christmas factor) by factor XIa (activated plasma thromboplastin antecedent) and a protease from Russell's viper venom. J Biol Chem. Mar 25; (6)– Kisiel W, Hermodson MA, Davie EW. Factor X activating enzyme from Russell's viper venom: isolation and characterization.

Biochemistry. Activation of bovine factor XII (Hageman factor) by plasma kallikrein. Studies of its activation by activated factor XII and of its inactivation by diisopropyl phosphofluoridate.

Specific adsorption of serine proteases on coated silica beads substituted with amidine derivatives.The book deals with all aspects of bovine mastitis, researchers from 4 continents shared in writing this book. species-specific risk factor studies, relying on accurate identification methods.Factor VII protein obtained by this method has only to times more activity in a one-stage clotting assay than in a coupled amidolytic assay (Seligsohn, U., Osterud, B., and Rapaport, S.

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