Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Francis Mainferme"'
Autor:
Anick Claessens, Simone Wattiaux-De Coninck, Michel Jadot, Franz Dubois, Robert Wattiaux, Francis Mainferme
Publikováno v:
Biochemical and Biophysical Research Communications. 223(2):353-359
Lamp II (for lysosomal associated membrane protein II) is an integral type I glycoprotein. It consists of a very large and heavily glycosylated luminal domain, a single transmembrane segment, and a short cytoplasmic tail. We show that in highly purif
Publikováno v:
European journal of cell biology. 81(12)
Summary Cathepsin C is a cysteine dipeptidyl-aminopeptidase. Active cathepsin C is found in lysosomes as a 200-kDa multimeric enzyme. Subunits constituting this assembly all arise from the proteolytic cleavage of a single precursor giving rise to thr
Autor:
Ciro Isidoro, Francis Mainferme, Robert Wattiaux, Daniela De Stefanis, Francesco M. Baccino, Marina Démoz
Publikováno v:
International journal of cancer. 60(1)
Both freshly-isolated rat hepatocytes and Morris hepatoma 7777 cells synthesized cathepsin D as a precursor that was either processed intracellulary to smaller mature forms or secreted into the medium. The pattern of mature enzyme forms was different
Autor:
Francis Mainferme, M. M. Gonze, Robert Wattiaux, Pierre J. Courtoy, P. Van Der Smissen, S. Wattiaux-De Coninck, L. De Waele, Jacqueline Thirion, Jean-Jacques Letesson
Publikováno v:
Endocytosis ISBN: 9783642842979
LGP10D10 is a 94 Kd glycoprotein recognized by a mouse monoclonal antibody directed against rat liver lysosomal membrane (Gonze et al., 1987). In rat liver and other tissues, lysosomes are heterogeneous. That results from the existence of probably di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c3848f525afe5f7a6cf3f84db857353
https://doi.org/10.1007/978-3-642-84295-5_29
https://doi.org/10.1007/978-3-642-84295-5_29
Transient membrane association of the precursors of cathepsin C during their transfer into lysosomes
Publikováno v:
The Biochemical journal. 275
Transport of the lysosomal enzyme cathepsin C was studied in Morris hepatoma 7777 cells. Subcellular fractions obtained after isopyenic centrifugation in sucrose gradients of labelled cell homogenates were sequentially extracted by hypo-osmotic shock
Publikováno v:
Cell Biology International Reports. 14:213
Synthesis, transport and processing of cathepsin C in Morris hepatoma 7777 cells and rat hepatocytes
Publikováno v:
European journal of biochemistry. 153(1)
The synthesis, transport and processing of cathepsin C was studied in Morris hepatoma 7777 cells by metabolic labelling, immunoprecipitation and characterization of labelled polypeptides by gel electrophoresis and fluorography. The largest detectable
Autor:
Francis Mainferme, Robert Wattiaux
Publikováno v:
European journal of biochemistry. 127(2)
The electrophoretic behaviour of rat-liver catalase in polyacrylamide gel depends on the subcellular fraction the enzyme was isolated from. Catalase extracted from the mitochondrial fraction is more anodic than catalase recovered from the unsedimenta
Autor:
Jean-Jacques Letesson, Simone Wattiaux-De Coninck, Francis Mainferme, Robert Wattiaux, Marie-Monique Gonze
Publikováno v:
Biochemical Society Transactions. 15:436-436
Autor:
Mainferme, Francis1, Wattiaux, Robert1
Publikováno v:
European Journal of Biochemistry. 10/1/82, Vol. 127 Issue 2, p343-346. 4p.