Zobrazeno 1 - 10
of 14
pro vyhledávání: '"C M, Noyes"'
Publikováno v:
Journal of Clinical Investigation. 68:1420-1426
Factor IXChapel Hill (Factor IXCH), an abnormal Factor IX molecule isolated from the plasma of a patient with mild hemophilia B, has previously been shown to exhibit delayed activation by Factor XIa and calcium. In this study, we have found that Fact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eaa342f557e29792759c17f6b759a8ef
https://doi.org/10.1172/jci110393
https://doi.org/10.1172/jci110393
Publikováno v:
The Journal of biological chemistry. 260(4)
Heparin cofactor II (Mr = 65,600) was purified 1800-fold from human plasma to further characterize the structural and functional properties of the protein as they compare to antithrombin III (Mr = 56,600). Heparin cofactor II and antithrombin III are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::daa5ae534ca028a3b620c64b0687aa00
https://pubmed.ncbi.nlm.nih.gov/3838304
https://pubmed.ncbi.nlm.nih.gov/3838304
Publikováno v:
The Journal of biological chemistry. 262(17)
Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent pyridoxal 5'-phosphate. Modification of antithrombin with limiting amounts of reag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::49acfd78243a8f93ca48cc6bdd7a8f27
https://pubmed.ncbi.nlm.nih.gov/3110143
https://pubmed.ncbi.nlm.nih.gov/3110143
Autor:
D L, Straight, G B, Sherrill, C M, Noyes, H G, Trapp, S F, Wright, H R, Roberts, R G, Hiskey, M J, Griffith
Publikováno v:
The Journal of biological chemistry. 260(5)
Activated human factor IX (factor IXa) was treated under mildly acidic conditions with a mixture of formaldehyde and morpholine. This reagent has been shown to react preferentially with gamma-carboxyglutamyl (Gla) residues and to convert these residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b3f6849ab7c3069209942abdb7d9bd83
https://pubmed.ncbi.nlm.nih.gov/3871774
https://pubmed.ncbi.nlm.nih.gov/3871774
Autor:
H G Trapp, Harold R. Roberts, Ernest Briet, M J Griffith, C M Noyes, L Breitkreutz, R L Lundblad
Two structurally different forms of activated human Factor IX (Factor IXa alpha and IXa beta) have been previously reported to have essentially identical clotting activity in vitro. Although it has been shown that activated Factor IX Chapel Hill, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e84b75ebcf74d6a9e226f2d95ce806eb
Publikováno v:
The Journal of biological chemistry. 263(8)
Previous studies from several laboratories have shown that thrombin is inactivated by tetranitromethane with the formation of nitrotyrosine. The inactivation is characterized by an apparently greater loss of fibrinogen-clotting activity than activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a81136952e0e8756fcc10fa5a06d845a
https://pubmed.ncbi.nlm.nih.gov/3346219
https://pubmed.ncbi.nlm.nih.gov/3346219
Publikováno v:
Thrombosis research. 27(5)
The cleavage of human prothrombin by partially purified Echis carinatus venom (ECV) was investigated in the present report. Incubation of prothrombin with ECV resulted in the rapid cleavage of prothrombin to alpha-thrombin, with the release of fragme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::105f97d0a7aa7a13eee04f0e84ee2ed8
https://pubmed.ncbi.nlm.nih.gov/6758184
https://pubmed.ncbi.nlm.nih.gov/6758184
Autor:
E M, Wilson, D H, Viskochil, R J, Bartlett, O A, Lea, C M, Noyes, P, Petrusz, D W, Stafford, F S, French
Publikováno v:
Progress in clinical and biological research.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0121c595b24d12ea4941910839c0337a
https://pubmed.ncbi.nlm.nih.gov/6175980
https://pubmed.ncbi.nlm.nih.gov/6175980
Publikováno v:
The Journal of biological chemistry. 261(11)
The present study has made use of a covalent cross-linking agent, dithiobis(succinimidylpropionate), to study the self-association of prothrombin and has demonstrated that the covalent dimerization reaction involves the gamma-carboxyglutamic acid reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ba75f70a47033ed8afcc6bf810b45122
https://pubmed.ncbi.nlm.nih.gov/3957915
https://pubmed.ncbi.nlm.nih.gov/3957915
Publikováno v:
The Journal of biological chemistry. 254(17)
The partial covalent structure of bovine beta-thrombin has been determined by the use of automated Edman degradation and carboxypeptidase digestion of the component polypeptide chains separated by gel filtration following either reduction and carboxy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7e786ca6ddb5079d92e0f75d74baf346
https://pubmed.ncbi.nlm.nih.gov/468839
https://pubmed.ncbi.nlm.nih.gov/468839