Zobrazeno 1 - 10
of 17
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4a10e8cfd331bf5c820499b6aaa0437
https://doi.org/10.1080/10731190600769164
https://doi.org/10.1080/10731190600769164
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0140d2dfb44651a02baa4d86595d13cd
https://doi.org/10.2174/157016405774641156
https://doi.org/10.2174/157016405774641156
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d77e0f656fabbf72a16ca6b0653f2e84
https://doi.org/10.1034/j.1399-3011.2000.00725.x
https://doi.org/10.1034/j.1399-3011.2000.00725.x
Akademický článek
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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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83d215d166ebc780c70d7a6c53fc11f2
https://pubmed.ncbi.nlm.nih.gov/20653337
https://pubmed.ncbi.nlm.nih.gov/20653337
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e5b7a6482de8146aa265902df1846d7
https://pubmed.ncbi.nlm.nih.gov/19653083
https://pubmed.ncbi.nlm.nih.gov/19653083
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67e342a8847d2380eaad80edcbbfc99a
https://pubmed.ncbi.nlm.nih.gov/19119852
https://pubmed.ncbi.nlm.nih.gov/19119852
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28de723248d3f6a417fbb2e94439093e
https://pubmed.ncbi.nlm.nih.gov/17381072
https://pubmed.ncbi.nlm.nih.gov/17381072
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3404e524f57665a96fd92f8e3b64298
https://pubmed.ncbi.nlm.nih.gov/12962322
https://pubmed.ncbi.nlm.nih.gov/12962322