Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Muthuchidambaram Prabhakaran"'
Publikováno v:
Artificial Cells, Blood Substitutes, and Biotechnology. 34:381-393
Surface decoration of hemoglobin (Hb) with six copies of PEG-5K employing thiolation mediated PEGylation platform neutralizes the vasoaconstricive activity of acellular Hb. The molecular size homogeneity of hexaPEGylated Hb, in spite of the fact that
Autor:
Mark D. Shenderovich, Cindy L. Fisher, Vladimir Tseitin, Michael J. Dudek, S. McDonald, Muthuchidambaram Prabhakaran, Kal Ramnarayan, Shankari Mylvaganam, R. Kodandapani, Jian Hua Zheng, G. Raghunathan
Publikováno v:
Current Proteomics. 2:233-258
Publikováno v:
The Journal of Peptide Research. 56:12-23
We report the amino acid sequence of a basic protein isolated from the snake venom of Naja naja atra. An automated Edman sequencer was used to determine the 65-residue sequence, aided by electrospray ionization/mass spectrometry. Online reduction and
Publikováno v:
Artificial cells, blood substitutes, and immobilization biotechnology. 39(2)
The propensity of site-specific carboxymethylation and propylation of Val-1(α) of Hb to attenuate the reductive hexaPEGylation-induced dissociation of tetramers has been investigated. Only reductive propylation of Val-1(α), which increases the stab
Autor:
Seetharama A. Acharya, Pedro Cabrales, Paul K. Smith, Fantao Meng, Marcos Intaglietta, Muthuchidambaram Prabhakaran, Amy G. Tsai, Belur N. Manjula
Publikováno v:
The protein journal. 28(5)
A new hexaPEGylated hemoglobin, (TCP-PEG5K)(6)-Hb (TCP, thiocarbamoyl phenyl) has been developed using PEG-phenyl-isothiocyanate and its vasoactivity and structure has been investigated. Of the six PEG5K chains of (TCP-PEG5K)(6)-Hb, 4 are conjugated
Autor:
Seetharama A. Acharya, Dongxia Li, Tao Hu, Belur N. Manjula, Muthuchidambaram Prabhakaran, Michael Brenowitz
Publikováno v:
Biochemistry. 48(3)
A hexaPEGylated hemoglobin (Hb), (Propyl-PEG5K)(6)-Hb, is essentially in alphabeta dimers (Hu et al. (2007) Biochem. J. 402, 143-151). In order to provide a biochemical insight into the tetramer-dimer dissociation of this PEGylated Hb, we prepared an
Autor:
Belur N. Manjula, Seetharama A. Acharya, Muthuchidambaram Prabhakaran, Parimala Nacharaju, Joel M. Friedman
Publikováno v:
Biochemistry. 46(15)
HexaPEGylated hemoglobin (Hb), a non-hypertensive Hb, exhibits high O2 affinity, which makes it difficult for it to deliver the desired levels of oxygen to tissues. The PEGylation of very low O2 affinity Hbs is now contemplated as the strategy to gen
Our recent studies on PEG–Hb [poly(ethylene glycol)–Hb] conjugates generated by thiolation-mediated maleimide-chemistry based PEGylation demonstrated that the vasoactivity of the PEG–Hb conjugates is a function of the configuration of the PEG c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd34e3c363b3036f872ae2e3c7020efc
https://europepmc.org/articles/PMC1316295/
https://europepmc.org/articles/PMC1316295/
Autor:
Philip D. Sun, Seetharama A. Acharya, Eric S. Peterson, Joel M. Friedman, Chien Ho, Ashok Malavalli, Muthuchidambaram Prabhakaran, Belur N. Manjula, Arthur Arnone
Publikováno v:
Journal of protein chemistry. 22(3)
The influence of allosteric effectors on the R-state (liganded) conformation of Tg-HbP (human hemoglobin Presbyterian expressed in transgenic pig) has been probed using a number of biophysical techniques, and the results have been compared with that
Autor:
Joel M. Friedman, Belur N. Manjula, Muthuchidambaram Prabhakaran, A. Seetharama Acharya, Ashok Malavalli
Publikováno v:
Protein engineering. 14(5)
The Asn108 beta-->Lys mutation in hemoglobin (HbPresbyterian mutation) endows a low O(2) affinity-inducing propensity to the protein. Introduction of a fumaryl cross-bridge between its two alpha 99 lysine residues also induces a low O(2) affinity int