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Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI)

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Standard

Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI). / Valnickova, Zuzana; Thaysen-Andersen, Morten; Højrup, Peter; Christensen, Trine; Sanggaard, Kristian W; Kristensen, Torsten; Enghild, Jan J.

I: B M C Biochemistry, Bind 10, 2009, s. 13.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Valnickova, Z, Thaysen-Andersen, M, Højrup, P, Christensen, T, Sanggaard, KW, Kristensen, T & Enghild, JJ 2009, 'Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI)', B M C Biochemistry, bind 10, s. 13. https://doi.org/10.1186/1471-2091-10-13

APA

Valnickova, Z., Thaysen-Andersen, M., Højrup, P., Christensen, T., Sanggaard, K. W., Kristensen, T., & Enghild, J. J. (2009). Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI). B M C Biochemistry, 10, 13. https://doi.org/10.1186/1471-2091-10-13

CBE

Valnickova Z, Thaysen-Andersen M, Højrup P, Christensen T, Sanggaard KW, Kristensen T, Enghild JJ. 2009. Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI). B M C Biochemistry. 10:13. https://doi.org/10.1186/1471-2091-10-13

MLA

Vancouver

Valnickova Z, Thaysen-Andersen M, Højrup P, Christensen T, Sanggaard KW, Kristensen T o.a. Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI). B M C Biochemistry. 2009;10:13. https://doi.org/10.1186/1471-2091-10-13

Author

Valnickova, Zuzana ; Thaysen-Andersen, Morten ; Højrup, Peter ; Christensen, Trine ; Sanggaard, Kristian W ; Kristensen, Torsten ; Enghild, Jan J. / Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI). I: B M C Biochemistry. 2009 ; Bind 10. s. 13.

Bibtex

@article{9ce94d90fa1b11de9c17000ea68e967b,
title = "Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI)",
abstract = "BACKGROUND: TAFI is a plasma protein assumed to be an important link between coagulation and fibrinolysis. The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. In light of these recent advances, we have characterized authentic bovine TAFI biochemically and compared it to human TAFI. RESULTS: The four N-linked glycosylation sequons within the activation peptide were all occupied in bovine TAFI, similar to human TAFI, while the sequon located within the enzyme moiety of the bovine protein was non-glycosylated. The enzymatic stability and the kinetic constants of TAFIa differed somewhat between the two proteins, as did the isoelectric point of TAFI, but not TAFIa. Equivalent to human TAFI, bovine TAFI was a substrate for transglutaminases and could be proteolytically cleaved by trypsin or thrombin/solulin complex, although small differences in the fragmentation patterns were observed. Furthermore, bovine TAFI exhibited intrinsic activity and TAFIa attenuated tPA-mediated fibrinolysis similar to the human protein. CONCLUSION: The findings presented here suggest that the properties of these two orthologous proteins are similar and that conclusions reached using the bovine TAFI may be extrapolated to the human protein.",
keywords = "Animals, Carboxypeptidase U, Cattle, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Fibrinolysis, Glycosylation, Humans, Isoelectric Point, Isoenzymes, Kinetics, Molecular Weight, Peptide Fragments, Polysaccharides, Substrate Specificity, Temperature, Trypsin",
author = "Zuzana Valnickova and Morten Thaysen-Andersen and Peter H{\o}jrup and Trine Christensen and Sanggaard, {Kristian W} and Torsten Kristensen and Enghild, {Jan J}",
year = "2009",
doi = "10.1186/1471-2091-10-13",
language = "English",
volume = "10",
pages = "13",
journal = "B M C Biochemistry",
issn = "1471-2091",
publisher = "BioMed Central Ltd.",

}

RIS

TY - JOUR

T1 - Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI)

AU - Valnickova, Zuzana

AU - Thaysen-Andersen, Morten

AU - Højrup, Peter

AU - Christensen, Trine

AU - Sanggaard, Kristian W

AU - Kristensen, Torsten

AU - Enghild, Jan J

PY - 2009

Y1 - 2009

N2 - BACKGROUND: TAFI is a plasma protein assumed to be an important link between coagulation and fibrinolysis. The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. In light of these recent advances, we have characterized authentic bovine TAFI biochemically and compared it to human TAFI. RESULTS: The four N-linked glycosylation sequons within the activation peptide were all occupied in bovine TAFI, similar to human TAFI, while the sequon located within the enzyme moiety of the bovine protein was non-glycosylated. The enzymatic stability and the kinetic constants of TAFIa differed somewhat between the two proteins, as did the isoelectric point of TAFI, but not TAFIa. Equivalent to human TAFI, bovine TAFI was a substrate for transglutaminases and could be proteolytically cleaved by trypsin or thrombin/solulin complex, although small differences in the fragmentation patterns were observed. Furthermore, bovine TAFI exhibited intrinsic activity and TAFIa attenuated tPA-mediated fibrinolysis similar to the human protein. CONCLUSION: The findings presented here suggest that the properties of these two orthologous proteins are similar and that conclusions reached using the bovine TAFI may be extrapolated to the human protein.

AB - BACKGROUND: TAFI is a plasma protein assumed to be an important link between coagulation and fibrinolysis. The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. In light of these recent advances, we have characterized authentic bovine TAFI biochemically and compared it to human TAFI. RESULTS: The four N-linked glycosylation sequons within the activation peptide were all occupied in bovine TAFI, similar to human TAFI, while the sequon located within the enzyme moiety of the bovine protein was non-glycosylated. The enzymatic stability and the kinetic constants of TAFIa differed somewhat between the two proteins, as did the isoelectric point of TAFI, but not TAFIa. Equivalent to human TAFI, bovine TAFI was a substrate for transglutaminases and could be proteolytically cleaved by trypsin or thrombin/solulin complex, although small differences in the fragmentation patterns were observed. Furthermore, bovine TAFI exhibited intrinsic activity and TAFIa attenuated tPA-mediated fibrinolysis similar to the human protein. CONCLUSION: The findings presented here suggest that the properties of these two orthologous proteins are similar and that conclusions reached using the bovine TAFI may be extrapolated to the human protein.

KW - Animals

KW - Carboxypeptidase U

KW - Cattle

KW - Chromatography, High Pressure Liquid

KW - Electrophoresis, Polyacrylamide Gel

KW - Enzyme Stability

KW - Fibrinolysis

KW - Glycosylation

KW - Humans

KW - Isoelectric Point

KW - Isoenzymes

KW - Kinetics

KW - Molecular Weight

KW - Peptide Fragments

KW - Polysaccharides

KW - Substrate Specificity

KW - Temperature

KW - Trypsin

U2 - 10.1186/1471-2091-10-13

DO - 10.1186/1471-2091-10-13

M3 - Journal article

C2 - 19416536

VL - 10

SP - 13

JO - B M C Biochemistry

JF - B M C Biochemistry

SN - 1471-2091

ER -