Zobrazeno 1 - 6
of 6
pro vyhledávání: '"F. C. Van Der Wiele"'
Autor:
J.A.F. Op den Kamp, Ben Roelofsen, L.L.M. Van Deenen, H. J. Vial, G.N. Moll, F. C. Van Der Wiele, G.H. de Haas, Arend J. Slotboom, Marie-Laure Ancelin
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1024:189-192
Pig pancreatic phospholipase A2 does not act on normal erythrocytes, but the membrane penetrating capacity is enhanced by the covalent attachment of one fatty acyl chain to Lys-116 of the enzyme. Taking advantage of the impaired packing of phospholip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fbfee2445fc923e1c53beca768b4948
https://doi.org/10.1016/0005-2736(90)90224-c
https://doi.org/10.1016/0005-2736(90)90224-c
Autor:
F. C. Van Der Wiele, A. M. M. Schreurs, Arend J. Slotboom, R. Dijkman, G.H. de Haas, W. Atsma
Publikováno v:
Biochemistry. 27:1683-1688
The lipid-binding domain of pancreatic phospholipases A2 contains a number of exposed, hydrophobic amino acid side chains that are involved in the binding of the enzyme to organized lipid-water interfaces. Besides these apolar residues, at least two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::871b5461cb7a890bbf8728c8feaecc27
https://doi.org/10.1021/bi00405a045
https://doi.org/10.1021/bi00405a045
Autor:
Ben Roelofsen, G.H. de Haas, J. Van Binsbergen, F. C. Van Der Wiele, W. Atsma, Arend J. Slotboom, D. Raykova, F. Radvanyi, M. Van Linde
Publikováno v:
Biochemistry. 27:1688-1694
Long-chain lecithins present in bilayer structures like vesicles or membranes are only very poor substrates for pancreatic phospholipases A2. This is probably due to the fact that pancreatic phospholipases A2 cannot penetrate into the densely packed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::95a4c2aabb068a4eeaa6cdbd6de2df2e
https://doi.org/10.1021/bi00405a046
https://doi.org/10.1021/bi00405a046
Autor:
F C, Van der Wiele, W, Atsma, B, Roelofsen, M, van Linde, J, Van Binsbergen, F, Radvanyi, D, Raykova, A J, Slotboom, G H, De Haas
Publikováno v:
Biochemistry. 27(5)
Long-chain lecithins present in bilayer structures like vesicles or membranes are only very poor substrates for pancreatic phospholipases A2. This is probably due to the fact that pancreatic phospholipases A2 cannot penetrate into the densely packed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::acdba74fa799ac488a1da136f73f7fe2
https://pubmed.ncbi.nlm.nih.gov/3130102
https://pubmed.ncbi.nlm.nih.gov/3130102
Autor:
M. G. Van Oort, G.H. de Haas, F. C. Van Der Wiele, Arend J. Slotboom, M. Van Linde, Ben Roelofsen, W. Atsma
Publikováno v:
Enzymes of Lipid Metabolism II ISBN: 9781468452143
This study deals with some kinetic properties of porcine pancreatic phospholipase A2 (PLA2) acting on neutral and anionic substrates. Short—chain diacylglycerosulfates possess a much higher affinity to the enzyme than the corresponding lecithins. A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ee618f39fabbaf96df46f4a966821837
https://doi.org/10.1007/978-1-4684-5212-9_16
https://doi.org/10.1007/978-1-4684-5212-9_16
Publikováno v:
Biochemistry. 27(5)
The lipid-binding domain of pancreatic phospholipases A2 contains a number of exposed, hydrophobic amino acid side chains that are involved in the binding of the enzyme to organized lipid-water interfaces. Besides these apolar residues, at least two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::735dd058d0a1d331968b3c84e96c4a89
https://pubmed.ncbi.nlm.nih.gov/3130101
https://pubmed.ncbi.nlm.nih.gov/3130101