Log in

Relevant bibliographies by topics / Carboxylase. Vitamine K

Contents

Journal articles
Dissertations / Theses
Book chapters
Conference papers

Academic literature on the topic 'Carboxylase. Vitamine K'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Carboxylase. Vitamine K.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Carboxylase. Vitamine K"

1

Sun, Yan-Mei, Da-Yun Jin, Rodney M. Camire, and Darrel W. Stafford. "Vitamin K epoxide reductase significantly improves carboxylation in a cell line overexpressing factor X." Blood 106, no. 12 (2005): 3811–15. http://dx.doi.org/10.1182/blood-2005-06-2495.

Full text

Abstract:

Previously we reported that we could increase the fraction of carboxylated factor X by reducing the affinity of the propeptide for its binding site on human gamma glutamyl carboxylase. We attributed this to an increased turnover rate. However, even with the reduced affinity propeptide, when sufficient overproduction of factor X is achieved, there is still a significant fraction of uncarboxylated recombinant factor X. We report here that the factor X of such a cell line was only 52% carboxylated but that the fraction of carboxylated factor X could be increased to 92% by coexpressing the recentl

APA, Harvard, Vancouver, ISO, and other styles

2

Darghouth, Dhouha, Kevin W. Hallgren, Rebecca L. Shtofman, et al. "Compound heterozygosity of novel missense mutations in the gamma-glutamyl-carboxylase gene causes hereditary combined vitamin K–dependent coagulation factor deficiency." Blood 108, no. 6 (2006): 1925–31. http://dx.doi.org/10.1182/blood-2005-12-010660.

Full text

Abstract:

AbstractHereditary combined vitamin K–dependent (VKD) coagulation factor deficiency is an autosomal recessive bleeding disorder associated with defects in either the γ-carboxylase, which carboxylates VKD proteins to render them active, or the vitamin K epoxide reductase (VKORC1), which supplies the reduced vitamin K cofactor required for carboxylation. Such deficiencies are rare, and we report the fourth case resulting from mutations in the carboxylase gene, identified in a Tunisian girl who exhibited impaired function in hemostatic VKD factors that was not restored by vitamin K administration

APA, Harvard, Vancouver, ISO, and other styles

3

Van Haarlem, L. J. M., M. M. W. Ulrich, H. C. Hemker, B. A. M. Soute, and C. Vermeer. "Isolation and partial characterization of a vitamin K-dependent carboxylase from bovine aortae." Biochemical Journal 245, no. 1 (1987): 251–55. http://dx.doi.org/10.1042/bj2450251.

Full text

Abstract:

Vitamin K-dependent carboxylase activity has been demonstrated in the crude microsomal fraction of the intima of bovine aortae. The procedure for the isolation of vessel wall carboxylase is a slight modification of the general preparation procedure for tissue microsomes. The highest activity of the non-hepatic enzyme was observed at 25 degrees C and hardly any NADH-dependent vitamin K reductase could be demonstrated. The optimal reaction conditions for both vessel wall as well as liver carboxylase were similar: 0.1 M-NaCl/0.05 M-Tris/HCl, pH 7.4, containing 8 mM-dithiothreitol, 0.4% 3-[(3-chol

APA, Harvard, Vancouver, ISO, and other styles

4

Fusaro, Maria, Giuseppe Cianciolo, Maria Luisa Brandi, et al. "Vitamin K and Osteoporosis." Nutrients 12, no. 12 (2020): 3625. http://dx.doi.org/10.3390/nu12123625.

Full text

Abstract:

Vitamin K acts as a coenzyme of carboxylase, catalyzing the carboxylation of several vitamin K dependent proteins. Beyond its well-known effects on blood coagulation, it also exerts relevant effects on bone and the vascular system. In this review, we point out the relevance of an adequate vitamin K intake to obtain sufficient levels of carboxylated (active form) vitamin K dependent proteins (such as Osteocalcin and matrix Gla protein) to prevent bone health. Another bone-related action of Vitamin K is being a ligand of the nuclear steroid and xenobiotic receptor (SXR). We also discuss the reco

APA, Harvard, Vancouver, ISO, and other styles

5

Pudota, B. Nirmala, Eric L. Hommema, Kevin W. Hallgren, Beth A. McNally, Susan Lee та Kathleen L. Berkner. "Identification of Sequences within the γ-Carboxylase That Represent a Novel Contact Site with Vitamin K-dependent Proteins and That Are Required for Activity". Journal of Biological Chemistry 276, № 50 (2001): 46878–86. http://dx.doi.org/10.1074/jbc.m108696200.

Full text

Abstract:

The vitamin K-dependent (VKD) carboxylase converts clusters of Glu residues to γ-carboxylated Glu residues (Glas) in VKD proteins, which is required for their activity. VKD precursors are targeted to the carboxylase by their carboxylase recognition site, which in most cases is a propeptide. We have identified a second tethering site for carboxylase and VKD proteins that is required for carboxylase activity, called the vitamin K-dependent protein site of interaction (VKS). Several VKD proteins specifically bound an immobilized peptide comprising amino acids 343–355 of the human carboxylase (CVY

APA, Harvard, Vancouver, ISO, and other styles

6

Cozzolino, Mario, Michela Mangano, Andrea Galassi, Paola Ciceri, Piergiorgio Messa, and Sagar Nigwekar. "Vitamin K in Chronic Kidney Disease." Nutrients 11, no. 1 (2019): 168. http://dx.doi.org/10.3390/nu11010168.

Full text

Abstract:

Vitamin K is a composite term referring to a group of fat-soluble vitamins that function as a cofactor for the enzyme γ-glutamyl carboxylase (GGCX), which activates a number of vitamin K-dependent proteins (VKDPs) involved in haemostasis and vascular and bone health. Accumulating evidence demonstrates that chronic kidney disease (CKD) patients suffer from subclinical vitamin K deficiency, suggesting that this represents a population at risk for the biological consequences of poor vitamin K status. This deficiency might be caused by exhaustion of vitamin K due to its high requirements by vitami

APA, Harvard, Vancouver, ISO, and other styles

7

Berg, Marian de Boer-van den, Henk H. W. Thijssen, and Cees Vermeer. "The In Vivo Effects of Oral Anticoagulants in Man: Comparison Between Liver and Non-Hepatic Tissues." Thrombosis and Haemostasis 59, no. 02 (1988): 147–50. http://dx.doi.org/10.1055/s-0038-1642744.

Full text

Abstract:

SummaryThe in vivo effects of oral anticoagulant therapy with 4–hydroxycoumarins on various vitamin K–dependent enzyme systems in man were compared. In hepatic microsomes obtained from donors who has been treated with 4–hydroxycoumarins for more than 6 months, the vitamin K 2,3 epoxide reductase activity and the DTT–dependent vitamin K quinone reductase activity were diminished to 35% and 20% of the corresponding normal values. In the non–hepatic tissues, only a small decrease in vitamin K 2,3 epoxide reductase activity could be demonstrated, while no differences were found in the vitamin K qu

APA, Harvard, Vancouver, ISO, and other styles

8

Coutu, Daniel L., Jian Wui Wu, Georges-Etienne Rivard, Mark D. Blostein та Jacques Galipeau. "Periostin Is a Previously Uncharacterised Vitamin K Dependent γ-Carboxyglutamic Acid (Gla) Containing Protein Expressed by Marrow-Derived Mesenchymal Stromal Cells." Blood 110, № 11 (2007): 1927. http://dx.doi.org/10.1182/blood.v110.11.1927.1927.

Full text

Abstract:

Abstract The modification of glutamic acid residues to g-carboxyglutamic acid (Gla) is a post-translational modification catalyzed by the vitamin K-dependent γ-glutamylcarboxylase enzyme. Despite ubiquitous expression of the γ-carboxylation machinery in mammalian tissues, only 12 Gla-containing proteins have so far been identified in humans. Because bone tissue is the second most abundant source of Gla-proteins after the liver, we sought to identify Gla proteins secreted by bone-marrow derived mesenchymal stromal cells (MSCs), a precursor to all non-hematopoietic cells in bones. We used a prot

APA, Harvard, Vancouver, ISO, and other styles

9

MORITA, Takashi. "Vitamin K-Dependent Carboxylase." Japanese Journal of Thrombosis and Hemostasis 1, no. 4 (1990): 362–66. http://dx.doi.org/10.2491/jjsth.1.362.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Suttie, J. W. "Vitamin K-Dependent Carboxylase." Annual Review of Biochemistry 54, no. 1 (1985): 459–77. http://dx.doi.org/10.1146/annurev.bi.54.070185.002331.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "Carboxylase. Vitamine K"

1

Soute, Bernardus Aloysius Maria. "Vitamin K-dependent carboxylase: growth to maturity." Maastricht : Maastricht : Universitaire Pers Maastricht ; University Library, Maastricht University [Host], 1993. http://arno.unimaas.nl/show.cgi?fid=6218.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Boer-van, den Berg Maria Anna Gerardina de. "Hepatic and non-hepatic vitamin K-dependent reactions." Maastricht : Maastricht : Rijksuniversiteit Limburg ; University Library, Maastricht University [Host], 1987. http://arno.unimaas.nl/show.cgi?fid=5356.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Ulrich, Magdalena Maria Wilhelmina. "Enzyme/substrate interactions of the vitamin K-dependent carboxylase." [Maastricht : Maastricht : Rijksuniversiteit Limburg] ; University Library, Maastricht University [Host], 1991. http://arno.unimaas.nl/show.cgi?fid=6207.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Darghouth, Dhouba Dalenda. "Etude d'un multi-deficit congénital en facteur de coagulation vitamine K-dépendant dans une famille tunisienne." Paris 7, 2006. http://www.theses.fr/2006PA077089.

Full text

Abstract:

La gamma-glutamyl carboxylase (gammaGC) et l'époxyde réductase (VKOR) sont des enzymes membranaires du réticulum endoplasmique, qui assurent la gamma-glutamyl carboxylation des facteurs vitamine K-dépendants (FVKD) : II, VII, IX, X, protéines C, S, Z. Une patiente tunisienne présentait un syndrome hémorragique avec multi-déficit en FVKD. L'enquête familiale a montré une transmission récessive, avec les parents et une sœur cliniquement indemnes, et un frère atteint. Nous avons amplifié par PCR et séquence les gènes de gammaGC et VKOR. Aucune mutation n'a été trouvée sur VKOR. Par contre la prop

APA, Harvard, Vancouver, ISO, and other styles

5

LARUE, VALERY. "Etude conformationnelle par rmn et modelisation moleculaire d'analogues de l'acide glutamique comme sonde de la carboxylase vitamine k dependante." Paris 6, 1996. http://www.theses.fr/1996PA066227.

Full text

Abstract:

Le mecanisme de la coagulation sanguine est un mecanisme fort complexe, de maturation proteique, qui fait intervenir une cascade de reactions enzymatiques et notamment des carboxylations vitamine k dependante de residus glu en gla. La reaction de carboxylation se fait en presence de la carboxylase (une enzyme transmembranaire), de la vitamine k, de co#2 et de dioxygene. En l'absence, de preparation purifiee de carboxylase, une approche passant par l'elaboration de substrats ou d'inhibiteurs peut permettre de mieux definir les caracteristiques du site actif de la carboxylase. Dans ce contexte,

APA, Harvard, Vancouver, ISO, and other styles

6

MAILLET, MAGALI. "Carboxylase dependant de la vitamine k : etude du mecanisme d'action du cofacteur et exploration du site actif par photomarquage." Paris 6, 1995. http://www.theses.fr/1995PA066662.

Full text

Abstract:

Nous avons etudie deux aspects de la carboxylation catalysee par la vitamine k. Le role du cofacteur a ete aborde par l'etude de l'incorporation et la localisation d'oxygene (#1#8o#2) au niveau de l'epoxyde de la vitamine k produit, a l'aide d'echantillons enrichis specifiquement. Apres optimisation des conditions experimentales (incorporation #1#8o#2 et extraction des produits), nous avons mis au point les conditions de sm/sm qui doivent permettre de mener l'analyse a son terme. En parllele, nous avons entame l'etude du site actif par marquage irreversible. La premiere tentative, basee sur la

APA, Harvard, Vancouver, ISO, and other styles

7

Sung, P. M. W. "Studies on the vitamin K dependent carboxylase." Thesis, University of Oxford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.354867.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Wood, Gary Michael. "Studies on vitamin K-dependent carboxylase." 1986. http://catalog.hathitrust.org/api/volumes/oclc/15540707.html.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Grossman, Carol Paula. "Inhibitors of the vitamin K-dependent carboxylase." 1991. http://catalog.hathitrust.org/api/volumes/oclc/24259287.html.

Full text

Abstract:

Thesis (Ph. D.)--University of Wisconsin--Madison, 1991.<br>Vita. Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

APA, Harvard, Vancouver, ISO, and other styles

10

Harbeck, Mark Christian. "Studies of the vitamin k-dependent carboxylase." 1992. http://catalog.hathitrust.org/api/volumes/oclc/28952870.html.

Full text

Abstract:

Thesis (Ph. D.)--University of Wisconsin--Madison, 1992.<br>Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 139-157).

APA, Harvard, Vancouver, ISO, and other styles

More sources

Book chapters on the topic "Carboxylase. Vitamine K"

1

Rost, S., A. Fregin, D. Koch, et al. "First Case of Compound Heterozygosity in the Gamma-Glutamyl Carboxylase Gene Causing Combined Deficiency of all Vitamin K-Dependent Blood Coagulation Factors." In 33rd Hemophilia Symposium. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18260-0_47.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

"Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase." In Vitamin K in Health and Disease. CRC Press, 2009. http://dx.doi.org/10.1201/9780849333927.ch4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Suttie, John W. "Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase." In VITAMIN K in Health and Disease. CRC Press, 2009. http://dx.doi.org/10.1201/9781420005110-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

"Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase." In Vitamin K in Health and Disease. CRC Press, 2009. http://dx.doi.org/10.1201/9781420005110.ch4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Berkner, Kathleen L., and Beth A. McNally. "[27] Purification of vitamin K-dependent carboxylase from cultured cells." In Methods in Enzymology. Elsevier, 1997. http://dx.doi.org/10.1016/s0076-6879(97)82117-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Houben, Roger J. T. J., Berry A. M. Soute, and Cees Vermeer. "[30] Assay of vitamin K-dependent carboxylase activity in hepatic and extrahepatic tissues." In Methods in Enzymology. Elsevier, 1997. http://dx.doi.org/10.1016/s0076-6879(97)82120-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Becker, Richard C., and Frederick A. Spencer. "Historical Perspectives in Hemostasis, Coagulation, and Fibrinolysis: A Foundation for Understanding Thrombotic Disorders and Developing Effective Treatment." In Fibrinolytic and Antithrombotic Therapy. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195155648.003.0005.

Full text

Abstract:

Hemostasis, the prompt cessation of bleeding at a site of vascular injury, is among the most fundamental physiologic and teleologically vital defense mechanisms in nature. Without a functionally intact hemostatic mechanism, death could ensue rapidly even after minor traumas associated with everyday life. In mammalian blood coagulation, regulated by a complex network of integrated biochemical events, five protease factors (f ) (fIIa [thrombin], fVIIa, fIXa, fXa, and protein C) interact with five cofactors (tissue factor, f VIIIa, fVa, thrombomodulin, and protein S) to regulate the generation of fibrin (Davidson et al., 2003). Although each component of the mammalian coagulation network has unique functional properties, available data based on gene organizations, protein structure, and sequence analysis suggest that it may have resulted from the reduplication and diversification of two gene structures over 400 million years ago. A vitamin K–dependent serine protease is composed of a γ-carboxylated glutamic acid (GLA) epidermal growth factor-like (EGF) 1–EGF 2-serine protease domain structure common to fVII, fIX, fX, and protein C, and the A1-A2-B-AB-C1-C2 domain structure common to fV and fVIII. Prothrombin is also a vitamin K–dependent serine protease; however, it contains kringle domains rather than EGF domains (suggesting a replacement during gene duplication and shuffling). Analyses of active site function amino acid residues reveal distinguishing characteristics of thrombin from other serine proteases, supporting its position as the ancestral blood enzyme (Krem and Cera, 2002; McLysaght et al., 2002). The rapid transformation of fluid blood to a gel-like substance (clot) has been a topic of great interest to scientists, physicians, and philosophers since the days of Plato and Aristotle ( Jewett, 1892; Lee, 1952). However, it was not until the beginning of the 18th century that blood clotting (coagulation) was appreciated as a means to stem blood loss from wounds (hemostasis) (Petit, 1731). As with other areas of science, the microscope played a pivotal role in the understanding of coagulation. In the mid-17th century, Marcello Malpighi separated the individual components of a blood clot into fibers, cells, and serum (Forester, 1956).

APA, Harvard, Vancouver, ISO, and other styles

8

Benton, Margaret E., and J. W. Suttie. "[32] Determination of site-specific γ-carboxyglutamic acid formation by vitamin K-dependent carboxylase utilizing de-γ-carboxy bone Gla protein as substrate." In Methods in Enzymology. Elsevier, 1997. http://dx.doi.org/10.1016/s0076-6879(97)82122-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Carboxylase. Vitamine K"

1

Van Haarlem, L. J. M., H. C. Hemker, B. A. M. Soute, and C. Vermeer. "GLA-CONTAINING PROTEINS FROM CALCIFIED HUMAN ATHEROSCLEROTIC PLAQUES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643747.

Full text

Abstract:

Vitamin K-dependent carboxylase activity has been detected in human andbovine vessel wall. Studies comparingthe carboxylases from liver and vessel wall revealed that the enzyme systems may be regarded as isoenzymes withwidely different substrate specificities. The carboxylated product of vessel wall carboxylase has not yet been identified, but it seems plausible that it will be found amongst the Gla-containing proteins which are abundantly present in calcified atherosclerotic plaques (Gla= gammacarboxyglutamicacid, the abnormal amino acid formed by vitamin K-dependent carboxylase). Therefore w

APA, Harvard, Vancouver, ISO, and other styles

2

Vermeer, C., BA M. Soute, and MM W. Ulrich. "IN VITRO CARBOXYLATION OF EXOGENOUS PROTEIN SUBSTRATES BY VITAMIN K-DEPENDENT CARBOXYLASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643994.

Full text

Abstract:

In vivo treatment of experimental animals with vitamin K-antagonists induces the accumulation of non-carboxylated coagulation factor precursors in the liver, where they are tightly bound to vitamin K-dependent carboxylase. If hepatic carboxylase is isolated from warfarin-treated animals, it is obtained therefore almost exclusively in the form of an enzyme/substrate complex. If carboxylase is prepared from non-treated animals, on the other hand, the resulting enzyme is predominantly substrate-free. Small substrates like F L E E L or decarboxylated osteocalcinare carboxylated equally well by bot

APA, Harvard, Vancouver, ISO, and other styles

3

Suttie, W. J., A. Cheung, and M. G. Wood. "ENZYMOLOGY OF THE VITAMIN K-DEPENDENT CARBOXYLASE: CURRENT STATUS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643991.

Full text

Abstract:

The vitamin K-dependent microsomal carboxylase converts glutamyl residues in precursor proteins to γ-carboxyglutamyl (Gla) residues in completed proteins. The enzyme activity is present in significant activities in most non-skeletal tissues but has been studied most extensively in rat and bovine liver. Early studies of the enzyme utilized bound precursors of vitamin K-dependent clotting factors as substrates for the enzyme and demonstrated that the enzyme requires the reduced form of vitamin K (vitamin KH2), O2, and CO2. Subsequent investigations have taken advantage of the observation that th

APA, Harvard, Vancouver, ISO, and other styles

4

Wallin, R., and S. R. Rannels. "IDENTIFICATION OF VITAMIN K-DEPENDENT CARBOXYLASE ACTIVITY AND EVIDENCE FOR PROTHROMBIN SYNTHESIS IN ALVEOLAR TYPE II CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644318.

Full text

Abstract:

Prothrombin precursors have been shown to be present in micro-somes from lung alveolar type II cells. Immunoblotting revealed two microsomal precursors of apparent mol. wt. 68 and 65 kDa. The 65 kDa protein appears to be the substrate for the vitamin Independent carboxylase. Fluorography of [14c]-labeled precursors of vitamin K-dependent proteins in lung microsomes shows that the lung has several precursors that are not found in the liver. Pulmonary macrophages appear to be devoid of vitamin K-dependent carboxylase activity. However, type II epithelial cells have significant activity and this

APA, Harvard, Vancouver, ISO, and other styles

5

Furis, B. C., M. J. Jorgensem, M. J. Rabiet, et al. "RECOGNITION SITE DIRECTING GAMMA-CARBOXYLATION RESIDES ON THE PROPEPTIDES OF FACTOR IX AND PROTRROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643992.

Full text

Abstract:

Factor IX and prothrombin vitamin K-dependent proteins that participate in blood coagulation undergo post-translationalmodification in which glutamic acid residues in the amino terminus of the protein are converted to gamma-carboxyglutamic acid residues. This modification confers divalent metal ion binding ability upon the proteins.As a consequence of binding divalent metal ions these proteins undergoconformational changes necessary for biological function.The vitamin K-dependent proteins are synthesized with an NH2-terminal extension. The region distal to the NH2-terminus of the mature protei

APA, Harvard, Vancouver, ISO, and other styles

6

O'hara, Patrick J., Frank A. Grant, A. Betty, J. Haldmen, and Mark J. Murray. "Structure of the Human Factor VII Gene." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643786.

Full text

Abstract:

Factor VII is a member of a family of vitamin K-dependent, gamma-carboxylated plasma protein which includes factor IX, factor X, protein C, protein S and prothrombin. Activated factor VII (factor Vila) is a plasma serine protease which participates in a cascade of reactions leading to the coagulation of blood. Two overlapping genomic clones containing sequences encoding human factor VII were isolated and characterized. The complete sequence of the gene was determined and found to span 12.8 kilobases. The mRNA for factor VII as demonstrated by cDNA cloning is polyadenylated at multiple sites bu

APA, Harvard, Vancouver, ISO, and other styles

7

Busby, S., K. Berkner, L. Halfpap, J. Gambee, and A. Kumar. "ALTERATION OF PROPTIDE SEQUENCE IMPAIRS BIOLOGICAL ACTIVITY OF HUMAN FACTOR VII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643784.

Full text

Abstract:

We have investigated the effect of altering the leader sequence of human factor VII on its biological activity. Factor VII is a vitamin K-dependent blood coagulation protein whose activity depends on the presence of gamma-carboxyglutamic acid (gla) residues in its amino terminal region. Since factor VII and other vitamin K-dependent proteins exhibit structural homology in the propeptide, it has been suggested that the propeptide is involved in gamma-carboxylation. Recently, two factor IX patients were identified with point mutations which prevented the processing of the propeptide and generate

APA, Harvard, Vancouver, ISO, and other styles

8

Gerna, M., and M. B. Donati. "HYPERCOAGULABILITY AND REDUCED SENSITIVITY TO WARFARIN IN RATS FOLLOWING CAFFEINE INTAKE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643399.

Full text

Abstract:

The effect(s) of caffeine Intake on cardiovascular functions are still a matter of debate. We have considered here the level of the prothrombin complex activity as a parameter of blood coagulability following caffeine Intake. The activity of the four vitamin K-dependent clotting factors (II, VII, IX and X) was tested after acute and chronic administration of high doses of caffeine. With a single administration of 50 mg/kg caffeine a statistically significant increase in the activity of factors VII, IX and X was observed. The increase lasted for 4, 3 and 2 days respectively. Factor II was not a

APA, Harvard, Vancouver, ISO, and other styles

9

Foster, D., B. Schach, M. Rudinsky, et al. "The Effect of Changes in the Leader Sequence of Human Protein C on Biosynthetic Processing and Gamma-Carboxylation." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643648.

Full text

Abstract:

Protein C is the precursor to a serine protease in plasma which contains gamma-carboxy glutamic acid and functions as a potent anticoagulant. Protein C shows considerable structural homology with the other vitamin K-dependent coagulation factors including prothrombin, factor VII, factor IX and factor X. This homology includes the putative pro-peptide region of the prepro leader sequences for these proteins, as well as the leader sequences for gamma-carboxylated proteins from bone. Deletion mutants have been constructed in the cDNA for human protein C in order to test the possibility that the p

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!