Zobrazeno 1 - 8
of 8
pro vyhledávání: '"P C, Esmon"'
Publikováno v:
The Journal of biological chemistry. 267(12)
The asparagine-linked sugar chains of blood coagulation factor VIII preparations purified from human plasma of blood group A donors and from the culture media of recombinant BHK cells were released as oligosaccharides by hydrazinolysis. These sugar c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5239b996d800602da89b1938a5675aab
https://pubmed.ncbi.nlm.nih.gov/1569060
https://pubmed.ncbi.nlm.nih.gov/1569060
Publikováno v:
Journal of Biological Chemistry. 259:10322-10327
N-linked oligosaccharides have been examined on glycoproteins accumulated in yeast mutants that are blocked at successive stages in the secretory pathway, and in a new mutant, gls1-1, deficient in removal of glucose from N-linked core oligosaccharide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04f037662c9c35c1259c46f5cdf36499
https://doi.org/10.1016/s0021-9258(18)90967-1
https://doi.org/10.1016/s0021-9258(18)90967-1
Publikováno v:
Journal of Biological Chemistry. 264:10493-10500
Human neutrophil elastase catalyzes the inactivation of antithrombin by a specific and limited proteinolytic cleavage. This inactivation reaction is greatly accelerated by an active anticoagulant heparin subfraction with high binding affinity for ant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a57221184720dbf3c32e1fa1bf35ad7
https://doi.org/10.1016/s0021-9258(18)81648-9
https://doi.org/10.1016/s0021-9258(18)81648-9
Publikováno v:
Journal of Bacteriology. 160:966-970
Yeast mutants that are conditionally blocked at distinctive steps in secretion and export of cell surface proteins have been used to monitor assembly of integral plasma membrane proteins. Mutants blocked in transport from the endoplasmic reticulum (s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0e8925df37449ca2be66212268f5b56
https://doi.org/10.1128/jb.160.3.966-970.1984
https://doi.org/10.1128/jb.160.3.966-970.1984
Publikováno v:
Journal of Biological Chemistry. 262:4387-4394
Yeast invertase forms a homo-octamer of core glycosylated subunits during assembly in the lumen of the endoplasmic reticulum. This form has been purified from mutant cells (sec18) in which transport of secreted proteins from the endoplasmic reticulum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4fc432d2007e6179dc81ff2e36371a8
https://doi.org/10.1016/s0021-9258(18)61360-2
https://doi.org/10.1016/s0021-9258(18)61360-2
Publikováno v:
XIth International Congress on Thrombosis and Haemostasis.
A panel of neutralizing and nonneutralizing monoclonal and polyclonal antibodies raised against human plasma FVIII and human recombinant FVIII was employed in Western blotting, activity inhibition and two-site ELISA studies to investigate structural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d090d3e3bc4dbbf79b97e28787a2fe89
https://doi.org/10.1055/s-0038-1644028
https://doi.org/10.1055/s-0038-1644028
Publikováno v:
The Journal of biological chemistry. 262(9)
Yeast invertase forms a homo-octamer of core glycosylated subunits during assembly in the lumen of the endoplasmic reticulum. This form has been purified from mutant cells (sec18) in which transport of secreted proteins from the endoplasmic reticulum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a33531b2c502b9881720c4e58d92030b
https://pubmed.ncbi.nlm.nih.gov/3031075
https://pubmed.ncbi.nlm.nih.gov/3031075
Publikováno v:
The Journal of biological chemistry. 264(18)
Human neutrophil elastase catalyzes the inactivation of antithrombin by a specific and limited proteinolytic cleavage. This inactivation reaction is greatly accelerated by an active anticoagulant heparin subfraction with high binding affinity for ant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6e0e9d756bef174251473e39d5af869a
https://pubmed.ncbi.nlm.nih.gov/2732232
https://pubmed.ncbi.nlm.nih.gov/2732232