Zobrazeno 1 - 10
of 10
pro vyhledávání: '"T M, Smudzin"'
Autor:
Philip J. Fay, T M Smudzin
Publikováno v:
Journal of Biological Chemistry. 267:13246-13250
Factor VIIIa is a heterotrimer of the factor VIII heavy chain-derived A1 and A2 subunits plus the factor VIII light chain-derived A3-C1-C2 subunit. While the A1 and A3-C1-C2 subunits can be isolated as a stable dimer, the A2 subunit is weakly associa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4f6c4f76e2944083567cab74bd27186d
https://doi.org/10.1016/s0021-9258(18)42201-6
https://doi.org/10.1016/s0021-9258(18)42201-6
Publikováno v:
Journal of Biological Chemistry. 266:20139-20145
Human factor VIII and factor VIIIa were proteolytically inactivated by activated protein C. Cleavages occurred within the heavy chain (contiguous A1-A2-B domains) of factor VIII and in the heavy chain-derived A1 and A2 subunits of factor VIIIa, where
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::818292716895db76cc68ca5527833412
https://doi.org/10.1016/s0021-9258(18)54901-2
https://doi.org/10.1016/s0021-9258(18)54901-2
Publikováno v:
Journal of Biological Chemistry. 266:8957-8962
Heterodimeric human factor VIII was proteolytically activated by catalytic levels of thrombin to yield the (labile) active cofactor factor VIIIa possessing an initial specific activity of approximately 80 units/microgram. Activation paralleled the ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::34dc60624bb01c7a345e05e4d20cb985
https://doi.org/10.1016/s0021-9258(18)31537-0
https://doi.org/10.1016/s0021-9258(18)31537-0
Autor:
Philip J. Fay, T M Smudzin
Publikováno v:
Journal of Biological Chemistry. 265:6197-6202
Factor VIII circulates in noncovalent complex with von Willebrand factor (vWf). The topography of this complex was evaluated by fluorescence energy transfer using factor VIII subunits modified with N-(1-pyrenyl)maleimide (NPM; fluorescence donor) and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18823f5afa8c18aa1f6a8f7d13435374
https://doi.org/10.1016/s0021-9258(19)39310-x
https://doi.org/10.1016/s0021-9258(19)39310-x
Autor:
P J, Fay, T M, Smudzin
Publikováno v:
The Journal of biological chemistry. 267(19)
Factor VIIIa is a heterotrimer of the factor VIII heavy chain-derived A1 and A2 subunits plus the factor VIII light chain-derived A3-C1-C2 subunit. While the A1 and A3-C1-C2 subunits can be isolated as a stable dimer, the A2 subunit is weakly associa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9e169260b4d0b2d6e59872ff0b9b9f0e
https://pubmed.ncbi.nlm.nih.gov/1618828
https://pubmed.ncbi.nlm.nih.gov/1618828
Publikováno v:
The Journal of biological chemistry. 266(30)
Human factor VIII and factor VIIIa were proteolytically inactivated by activated protein C. Cleavages occurred within the heavy chain (contiguous A1-A2-B domains) of factor VIII and in the heavy chain-derived A1 and A2 subunits of factor VIIIa, where
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d383d11f5d997b1fde94afebb01e725d
https://pubmed.ncbi.nlm.nih.gov/1939075
https://pubmed.ncbi.nlm.nih.gov/1939075
Publikováno v:
The Journal of biological chemistry. 266(14)
Heterodimeric human factor VIII was proteolytically activated by catalytic levels of thrombin to yield the (labile) active cofactor factor VIIIa possessing an initial specific activity of approximately 80 units/microgram. Activation paralleled the ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6b1438033862078366746279df58bbcb
https://pubmed.ncbi.nlm.nih.gov/1902833
https://pubmed.ncbi.nlm.nih.gov/1902833
Autor:
P J, Fay, T M, Smudzin
Publikováno v:
The Journal of biological chemistry. 265(11)
Factor VIII circulates in noncovalent complex with von Willebrand factor (vWf). The topography of this complex was evaluated by fluorescence energy transfer using factor VIII subunits modified with N-(1-pyrenyl)maleimide (NPM; fluorescence donor) and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::169687c2e450a26765e4c6aec46d49bf
https://pubmed.ncbi.nlm.nih.gov/2108154
https://pubmed.ncbi.nlm.nih.gov/2108154
Autor:
Philip J. Fay, T M Smudzin
Publikováno v:
Journal of Biological Chemistry. 264:14005-14010
Human factor VIII circulates as a series of active heterodimers composed of a light chain (83 kDa) linked by divalent metal ion(s) to a variable sized heavy chain (93-210 kDa). Purified factor VIII subunits were modified with sulfhydryl-specific fluo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::347294a5e6a869f2f6184fb6bc7f133d
https://doi.org/10.1016/s0021-9258(18)71633-5
https://doi.org/10.1016/s0021-9258(18)71633-5
Autor:
P J, Fay, T M, Smudzin
Publikováno v:
The Journal of biological chemistry. 264(24)
Human factor VIII circulates as a series of active heterodimers composed of a light chain (83 kDa) linked by divalent metal ion(s) to a variable sized heavy chain (93-210 kDa). Purified factor VIII subunits were modified with sulfhydryl-specific fluo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b08e41979f290e872c8253634c20540c
https://pubmed.ncbi.nlm.nih.gov/2503509
https://pubmed.ncbi.nlm.nih.gov/2503509