Zobrazeno 1 - 10
of 35
pro vyhledávání: '"I. Bosc-Bierne"'
Autor:
V. Patry, M. Guyader, B. Couderc, Véronique Baldin, Béatrix Bugler, A. M. Roman, Gérard Bouche, H. Prats, I. Bosc‐Bierne, François Amalric
Publikováno v:
ResearcherID
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce131331f3a475f912377b2f571c7ceb
https://doi.org/10.1111/j.1749-6632.1991.tb49023.x
https://doi.org/10.1111/j.1749-6632.1991.tb49023.x
Autor:
B, Gabriel, V, Baldin, A M, Roman, I, Bosc-Bierne, J, Noaillac-Depeyre, H, Prats, J, Teissié, G, Bouche, F, Amalric
Publikováno v:
Methods in enzymology. 198
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fdea0b87b8fb1e346732dec1268be77e
https://pubmed.ncbi.nlm.nih.gov/1857237
https://pubmed.ncbi.nlm.nih.gov/1857237
Primary cultures of adult bovine aortic endothelial (ABAE) cells require bFGF to grow. G1-arrested cells, obtained after 48 h without serum and bFGF, were found to enter S phase and grow synchronously for at least two generations on addition of bFGF.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1333bfb86fd5657eb02568d3d780dd3
https://europepmc.org/articles/PMC551843/
https://europepmc.org/articles/PMC551843/
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 998:158-166
To understand the mechanism by which colipase acts as a protein cofactor for anchoring pancreatic lipase at triacylglycerol/water interface, we have used an immunochemical approach. Ten monoclonal antibodies (Mabs) against porcine pancreatic procolip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfb032b8b76e6189f69f906e2957ae52
https://doi.org/10.1016/0167-4838(89)90268-9
https://doi.org/10.1016/0167-4838(89)90268-9
Publikováno v:
Biochimie. 63:227-234
Horse pancreatic lipase has been purified from tissue homogenates. Molecular and catalytic properties of horse lipase are comparable to those of the pancreatic lipases previously isolated. Kinetic studies of the inhibition of horse lipase activity by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::258f01b16f0853a6bdba1c5bd1fb92fc
https://doi.org/10.1016/s0300-9084(81)80196-4
https://doi.org/10.1016/s0300-9084(81)80196-4
Autor:
Louis Sarda, Patrick J. Cozzone, A. Kamoun, Robert Kaptein, I. Bosc-Bierne, J. Rathelot, P. Canioni
Publikováno v:
Biochimica et Biophysica Acta %28BBA%29-Protein Structure and Molecular Enzymology, 671(2), 155-163
Porcine and equine colipases have been submitted to mild tryptic digestion. Proteolysis occurs at the Arg5Gly6 bond with the loss of the N-terminal pentapeptide. Studies of native and trypsin-treated colipases by circular dichroism and laser chemi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d1b3678df4c72b0226fb32615bae746
https://doi.org/10.1016/0005-2795(81)90129-x
https://doi.org/10.1016/0005-2795(81)90129-x
Publikováno v:
Biochimie. 66(5)
Purified antibodies raised against chicken colipase were coupled to Sepharose 4B and colipase was isolated in a single step by immunoaffinity chromatography from an extract of chicken pancreas prepared under conditions where trypsin activation is avo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4520a9498f03446946d6f6d7933aea4b
https://pubmed.ncbi.nlm.nih.gov/6547861
https://pubmed.ncbi.nlm.nih.gov/6547861
Publikováno v:
Biochimica et biophysica acta. 794(1)
Lipase and colipase have been purified to homogeneity from chicken pancreatic tissue. The enzyme has a molecular weight (48 000) and catalytic properties similar to those of pancreatic lipase from higher mammals. Hydrolysis of triolein by chicken lip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62b66633a108032f741fe04044966911
https://pubmed.ncbi.nlm.nih.gov/6733130
https://pubmed.ncbi.nlm.nih.gov/6733130
Publikováno v:
Biochimica et biophysica acta. 744(1)
Pure colipase was prepared by immunoaffinity chromatography from porcine and human pancreatic juice. A single form of the porcine colipase was obtained, having the structural and biological properties of previously characterized porcine procolipase A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d721965b42bad256fc078313186a38eb
https://pubmed.ncbi.nlm.nih.gov/6830821
https://pubmed.ncbi.nlm.nih.gov/6830821
Autor:
J. Rathelot, Louis Sarda, Guy Bechis, Paul Canioni, Jana Gregoire, R. Julien, Hervé Rochat, I. Bosc-Bierne
Publikováno v:
Biochimica et biophysica acta. 667(2)
Colipase has been isolated from acidic extracts of chicken pancreatic tissue homogenized with Triton X-100. The cofactor fully activates bile salt inhibited mammalian lipases. The amino terminal sequence of the avian protein has been determined up to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::caadb91a7d5d068a280b00b54bfa1dc2
https://pubmed.ncbi.nlm.nih.gov/7213802
https://pubmed.ncbi.nlm.nih.gov/7213802