Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Mahdiyeh Mashahdi-keshtiban"'
Publikováno v:
Advanced Pharmaceutical Bulletin, Vol 11, Iss 4, Pp 728-738 (2021)
Purpose: This study focuses on the effect of length and structure of attached polyethylene glycol (PEG) chain on hydrodynamic radius (Rh ) and chromatographic retention of PEGylated protein. To this aim human serum albumin (HSA) as a standard protein
Externí odkaz:
https://doaj.org/article/6998fafe4d8845fe8aa9827a87361955
Autor:
Parvin Akbarzadehlaleh, Mona Mirzaei, Mahdiyeh Mashahdi-Keshtiban, Karim Shamsasenjan, Hamidreza Heydari
Publikováno v:
Advanced Pharmaceutical Bulletin, Vol 6, Iss 3, Pp 309-317 (2016)
Human serum albumin (HSA) is a non-glycosylated, negatively charged protein (Mw: about 65-kDa) that has one free cystein residue (Cys 34), and 17 disulfide bridges that these bridges have main role in its stability and longer biological life-time (15
Externí odkaz:
https://doaj.org/article/9085c2ebb59b4286a01ec2014edf10de
Publikováno v:
Advanced Pharmaceutical Bulletin
Advanced Pharmaceutical Bulletin, Vol 11, Iss 4, Pp 728-738 (2021)
Advanced Pharmaceutical Bulletin, Vol 11, Iss 4, Pp 728-738 (2021)
Purpose: This study focuses on the effect of length and structure of attached polyethylene glycol (PEG) chain on hydrodynamic radius (Rh ) and chromatographic retention of PEGylated protein. To this aim human serum albumin (HSA) as a standard protein
Autor:
Mahdiyeh Mashahdi-keshtiban, Parvin Akbarzadehlaleh, Karim Shamsasenjan, Hamidreza Heydari, Mona Mirzaei
Publikováno v:
Advanced Pharmaceutical Bulletin, Vol 6, Iss 3, Pp 309-317 (2016)
Human serum albumin (HSA) is a non-glycosylated, negatively charged protein (Mw: about 65-kDa) that has one free cystein residue (Cys 34), and 17 disulfide bridges that these bridges have main role in its stability and longer biological life-time (15