Zobrazeno 1 - 10
of 196
pro vyhledávání: '"de Haas Gh"'
Autor:
de Haas Gh, R. Dijkman, Rolf Boelens, Robert Kaptein, van den Berg B, Hubertus M. Verheij, Marco Tessari
Publikováno v:
Nature Structural & Molecular Biology. 2:402-406
It has long been proposed that the higher activity of phospholipase A2 (PLA2) for substrates presented as multimolecular aggregates compared to dispersed molecules (interfacial activation) arises due to a conformational change in the enzyme. X-ray st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0345ec6aae352906dbcf1e094bc4f17
https://doi.org/10.1038/nsb0595-402
https://doi.org/10.1038/nsb0595-402
Publikováno v:
Biochemistry. 20:1584-1591
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c438981e791bbcf70748967690bbe758
https://doi.org/10.1021/bi00509a027
https://doi.org/10.1021/bi00509a027
Publikováno v:
Biochemistry. 21:1345-1352
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e7cb46ded6a7c60e404676a2e5cb3701
https://doi.org/10.1021/bi00535a037
https://doi.org/10.1021/bi00535a037
Publikováno v:
Biochemistry. 22:5353-5358
The negatively charged detergents S-n-alka-noylthioglycol sulfates (C8, C9, and C10) are substrates for porcine pancreatic phospholipase A2 and its zymogen. At pH 6.0 and detergent concentrations up to 0.08 X critical micelle concentration (cmc), the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e0be5cc7b21a68aa16a6a4ec68fd047
https://doi.org/10.1021/bi00292a015
https://doi.org/10.1021/bi00292a015
Publikováno v:
Biochemistry. 18:580-586
The interaction between porcine pancreatic phospholipase A2 and a homogeneous population of micelles of the subtrate analogue n-hexadecylphosphorylcholine containing 155 lipid monomers was studied by light scattering, equilibrium gel filtration, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a51b1ee2ff30ce5b45cc750210f8a11
https://doi.org/10.1021/bi00571a005
https://doi.org/10.1021/bi00571a005
Publikováno v:
Biochemistry. 28(3)
The substrate specificity of Escherichia coli outer membrane phospholipase A was analyzed in mixed micelles of lipid with deoxycholate or Triton X-100. Diglycerides, monoglycerides, and Tweens 40 and 85 in Triton X-100 are hydrolyzed at rates compara
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e56181402c4c73e345f7fff6c67174d
https://pubmed.ncbi.nlm.nih.gov/2653433
https://pubmed.ncbi.nlm.nih.gov/2653433
Autor:
Götz F, Deveer Am, Hubertus M. Verheij, Tjeenk Ml, R. Dijkman, de Haas Gh, van Oort Mg, Wenzig E
Publikováno v:
Biochemistry. 28(24)
The Staphylococcus hyicus lipase gene has been cloned and expressed in Staphylococcus carnosus. From the latter organism the enzyme was secreted into the medium as a protein with an apparent molecular mass of 86 kDa. This protein was purified, and th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::475c648ee735890d54b0927ca4570c23
https://pubmed.ncbi.nlm.nih.gov/2611229
https://pubmed.ncbi.nlm.nih.gov/2611229
Publikováno v:
Biochemistry. 20(14)
Porcine pancreatic phospholipase A2 interacts with micelles of the substrate analogue n-octadecylphosphocholine to form a specific complex over considerably wide concentration ranges of both lipid and protein. UV absorption difference spectroscopy me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c416906430e8d5e0a27b5f585eba24b
https://pubmed.ncbi.nlm.nih.gov/7284310
https://pubmed.ncbi.nlm.nih.gov/7284310
Publikováno v:
Hoppe-Seyler's Zeitschrift fur physiologische Chemie. 361(4)
Reduction of porcine pancreatic phospholipase A2 with 2-mercaptoethanol in the presence of 6M guanidinium hydrocholoride or 8M urea resulted in the complete disruption of all seven disulfide bridges and the concomitant loss of all enzymatic activity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::441292fd08c4d12d92592371a56ff48a
https://pubmed.ncbi.nlm.nih.gov/7189740
https://pubmed.ncbi.nlm.nih.gov/7189740
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