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Nieuwenhuizen, W. (author), Oomens, A. (author), de Haas, G.H. (author), Gezondheidsorganisatie TNO Gaubius instituut TNO (author)
The purification of two different forms of prephospholipase A_2 from porcine pancreas is described in the accompanying paper. One of these has an activation peptide with the sequence <Glu‐Glu‐Gly‐Ile‐Ser‐Ser‐Arg and is designated form II; the other form has Ser‐Ser‐Arg as activation peptide and is designated form I. The Km and kcat values for...
article 1973
document
Nieuwenhuizen, W. (author), Steenbergh, P. (author), de Haas, G.H. (author), Gezondheidsorganisatie TNO Gaubius Instituut TNO (author)
Prephospholipase A_2, when isolated via the procedure described previously, by us in 1968, has pyroglutamic acid as the N‐terminal amino acid. However, this could be an artifact due to the drastic conditions of one of the early stages of the purification. Therefore a milder procedure has been developed in order to check whether or not...
article 1973
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van Ruijven-Vermeer, I.A.M. (author), Nieuwenhuizen, W. (author), Nooijen, W.J. (author), Gaubius instituut TNO (author)
The authors studied the binding of Ca to rat fibrinogen and plasmic fibrin(ogen) degradation products by means of equilibrium dialysis with special reference to the protective effect of Ca2+ in the plasmic degradation of fibrinogen. Direct binding studies demonstrate that rat fibrinogen and the plasmic degradation products D(cate) and D-dimer...
article 1978
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Gaubius instituut TNO (author), van Ruijven-Vermeer, I.A.M. (author), Nieuwenhuizen, W. (author)
Rat fibrinogen was purified from rat plasma by using lysine-Sepharose chromatography, repeated precipitation with 25%-satd. (HN4)2SO4 and gel chromatography on Sepharose 6B. To minimize proteolytic activity, rats were injected intravenously with Trasylol before bleeding and the collected blood was treated with Trasylol and di-isopropyl...
article 1978
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Nieuwenhuizen, W. (author), Vermond, A. (author), Nooijen, W.J. (author), Haverkate, F. (author), Gaubius Instituut TNO (author)
Here the results obtained with human fibrinogen and its degradation products are reported. Our results differ from those obtained in (9) but strongly support model suggested earlier by us for Ca2(+)-binding by rat fibrinogen. Chemicals/CAS: calcium, 7440-70-2; fibrin, 9001-31-4; fibrinogen, 9001-32-5; Calcium, 7440-70-2; Fibrin, 9001-31-4;...
article 1979
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Nieuwenhuizen, W. (author), Vermond, A. (author), Haverkate, F. (author), Gaubius instituut TNO (author)
Experiments have been carried out with fibrinogen and with purified degradation products of fibrinogen and fibrin which demonstrate that the structure of D fragments obtained after prolonged plasmin digestion is influenced by several factors in the media. The previously described protective effect of calcium ions on the ??-chain carboxy...
article 1981
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Nieuwenhuizen, W. (author), Gravesen, M. (author), Gaubius instituut TNO (author)
Early plasmin degradation products (X fragments) of human fibrinogen were prepared in the presence of calcium-ions or EGTA, and purified on Sepharose 6B-CL. X fragments were characterized with respect to amino-terminal amino acids, polypeptide-chain composition, anticlotting properties and calcium-binding. Amino-terminal amino acids were alanine...
article 1981
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Nieuwenhuizen, W. (author), Voskuilen, M. (author), Hermans, J. (author), Gaubius instituut TNO (author)
The present study was undertaken as a step to delineate further the localization of the calcium-binding sites in fibrinogen and to assess the anticlotting properties of fibrinogen degradation products. To this purpose, fragments Y were prepared by plasmin digestion of human fibrinogen in the presence of added Ca2+, and purified. We found that,...
article 1982
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Princen, J.G.M. (author), Selten, G.C.M. (author), Selten-Versteegen, A.E. (author), Mol-Backx, G.P.B.M. (author), Nieuwenhuizen, W. (author), Yap, S.H. (author), Gaubius Instituut TNO (author)
article 1982
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Verheijen, J.H. (author), Nieuwenhuizen, W. (author), Wijngaards, G. (author), Gaubius instituut TNO (author)
Tissue activator-mediated plasminogen activation is potentiated both by fibrin and by some soluble fibrin(ogen) fragments. The potentiating effect of the different fragments decreases in the order fibrin monomer > D-dimer > Y > D EGTA > Dcate > X. Fibrinogen and the fragments Ecate, E EGTA and E fibrin have almost no effect. The existence of a...
article 1982
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Nieuwenhuizen, W. (author), Haverkate, F. (author), Gaubius Instituut TNO (author)
Chemicals/CAS: fibrinogen, 9001-32-5; calcium, 7440-70-2; Calcium, 7440-70-2; Fibrinogen, 9001-32-5
article 1983
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Nieuwenhuizen, W. (author), Rijken, D.C. (author), Traas, D.W. (author), Gaubius Instituut TNO (author)
Disbalance between clot formation (coagulation) and dissolution (fibrinolysis) can cause thrombotic or bleeding events, depending on which of the two processes predominates. During fibrinolysis, insoluble fibrin is degraded to soluble fragments by plasmin, which can be formed by activation of plasminogen by tissue-type plasminogen activator (t...
conference paper 1984
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Haverkate, F. (author), Koopman, J. (author), Koppert, P. (author), Nieuwenhuizen, W. (author), Gaubius Instituut TNO (author)
Abstract
article 1984
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Haverkate, F. (author), Nieuwenhuizen, W. (author), Gaubius Instituut TNO (author)
Chemicals/CAS: calcium chloride, 10043-52-4; calcium, 7440-70-2; citric acid, 126-44-3, 5949-29-1, 77-92-9, 8002-14-0; edetic acid, 150-43-6, 60-00-4
article 1984
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Haverkate, F. (author), Koopman, J. (author), Koppert, P. (author), Nieuwenhuizen, W. (author), Gaubius Institute, Health Research Division TNO, 2313 AD Leiden, Netherlands (author)
article 1985
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Princen, H. (author), Moshage, H. (author), Emeis, J. (author), de Haard, J. (author), Nieuwenhuizen, W. (author), Yap, S.H. (author), Gaubius Instituut TNO (author)
Abstract
article 1985
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Koppert, P.W. (author), Huijsmans, C.M.G. (author), Nieuwenhuizen, W. (author), Gaubius instituut TNO (author)
Spleen cells of BALB/c mice, immunized with fragments Y of normal human fibrinogen, were fused with P3 x 63 Ag 8653 myeloma cells. A clone was found which produces monoclonal antibodies (Mab-Y18) of the IgM?? type. Mab-Y18 is immunoreactive with normal human fibrinogen, and its fragments X, Y, N-terminal disulphide knot, A??-chain, and A??...
article 1985
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Koopman, J. (author), Haverkate, F. (author), Koppert, P. (author), Nieuwenhuizen, W. (author), Brommer, E.J.P. (author), Gaubius Instituut TNO (author)
Abstract.
article 1985
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Koppert, P.W. (author), Koopman, J. (author), Haverkate, F. (author), Nieuwenhuizen, W. (author), Gaubius instituut TNO (author)
Balb/c mice were immunized with a mixture of fibrin degradation products (XDPs) prepared by complete lysis of a human bloot clot by tissue-type plasminogen activator and purified by immunoaffinity chromatography. Spleen cells of the mice were fused with P3 x 63 Ag 8653 myeloma cells. A clone (FDP 14) was selected that produces monoclonal...
article 1986
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Koppert, P.W. (author), Hoegee-de Nobel, E. (author), Nieuwenhuizen, W. (author), Gezondheidsorganisatie TNO Gaubius Instituut TNO (author)
Abstract.
article 1987
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