Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Richard S. Blackmore"'
Autor:
Thomas P Hopp, Klaudyna Spiewak, Maura-Ann H Matthews, Zafeiria Athanasiou, Richard S Blackmore, Gary A Gelbfish
Publikováno v:
PLoS ONE, Vol 17, Iss 5, p e0268537 (2022)
When bovine lactoferrin (bLF) contacts human vaginal fluid (VF) it is subjected to proteolytic degradation. This report describes fragmentation patterns of bLF dosed vaginally in clinical trials or incubated ex vivo with VF. A consensus pattern of fr
Externí odkaz:
https://doaj.org/article/01387d8f05f147a98dc6c0c26fbbd29c
Autor:
Thomas P. Hopp, Maura-Ann H. Matthews, Klaudyna Spiewak, Zafeiria Athanasiou, Richard S. Blackmore, Gary A. Gelbfish
This report describes proteolytic fragmentation and clearance of bovine lactoferrin (bLF) upon intravaginal administration in premenopausal women. Solid dose tablet formulations (MTbLF) progressed through 3 phases, Pre-dissolution, Dissolution, and W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf53f20f7aad59acc74af9823234c926
https://doi.org/10.21203/rs.3.rs-1912821/v1
https://doi.org/10.21203/rs.3.rs-1912821/v1
Autor:
Thomas P, Hopp, Maura-Ann H, Matthews, Klaudyna, Spiewak, Zafeiria, Athanasiou, Richard S, Blackmore, Gary A, Gelbfish
Publikováno v:
Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine.
This report describes proteolytic fragmentation and clearance of bovine lactoferrin (bLF) upon intravaginal administration in premenopausal women. Tablet formulations (MTbLF) containing 300 mg of bLF progressed through three phases: Pre-Dissolution,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f66f25a529c6eccbeacb593eba11e793
https://pubmed.ncbi.nlm.nih.gov/36580179
https://pubmed.ncbi.nlm.nih.gov/36580179
Autor:
Michael M. C. Sun, Kevin S. Beam, Michael Torgov, Stephen C. Alley, Nathan C. Ihle, Kevin J. Hamblett, Peter D. Senter, Charles G. Cerveny, Felicia G. M. Handley, Richard S. Blackmore
Publikováno v:
Bioconjugate Chemistry. 16:1282-1290
Site-specific conjugation of small molecules and enzymes to monoclonal antibodies has broad utility in the formation of conjugates for therapeutic, diagnostic, or structural applications. Precise control over the location of conjugation would yield h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bb1e40170f1366ced0d48d8b482b569
https://doi.org/10.1021/bc050201y
https://doi.org/10.1021/bc050201y
Publikováno v:
Applied and Environmental Microbiology. 63:4313-4320
Accumulation of soluble recombinant hemoglobin (rHb1.1) in Escherichia coli requires proper protein folding, prosthetic group (heme) addition, and subunit assembly. This served as a new model system for the study of the effects of temperature, protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f616f46a0d435e529cf462a013963b16
https://doi.org/10.1128/aem.63.11.4313-4320.1997
https://doi.org/10.1128/aem.63.11.4313-4320.1997
Publikováno v:
Journal of Biological Chemistry. 267:10950-10955
Ligand binding reactions and the relation between redox state and ligand binding in the hexa-heme nitrite reductase of Wolinella succinogenes have been studied using laser flash photolysis. On a picosecond time scale, a rapid excursion was observed c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a14b945595edba3729fddb68f49685b
https://doi.org/10.1016/s0021-9258(19)49858-x
https://doi.org/10.1016/s0021-9258(19)49858-x
Publikováno v:
Journal of Biological Chemistry. 266:19245-19249
The formation and disappearance of a photosensitive species during the reaction of reduced cytochrome c oxidase (putatively a3II.O2), EC 1.9.3.1, has been followed by (a) mixing a3II.CO with O2 in a stopped flow apparatus; (b) initiating the oxygen-o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcb59b23bdf6a864e36eafc523fd7dce
https://doi.org/10.1016/s0021-9258(18)54989-9
https://doi.org/10.1016/s0021-9258(18)54989-9
Publikováno v:
Journal of Biological Chemistry. 266:13097-13102
The kinetics of CO and NO recombination with the giant approximately 3600-kDa hexagonal bilayer hemoglobin of Lumbricus terrestris and its subunits, the approximately 200-kDa dodecamer of globin chains (3 x chains (I + II + III + IV] (see preceding p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7562e375d4ac7a9ff3bb4a5064fe6d49
https://doi.org/10.1016/s0021-9258(18)98809-5
https://doi.org/10.1016/s0021-9258(18)98809-5
Autor:
Richard S. Blackmore, Quentin H. Gibson, John S. Olson, Guy Dodson, Stephen J. Smerdon, Theodore E. Carver, Anthony J. Wilkinson
Publikováno v:
Biochemistry. 30:6252-6260
Site-directed mutagenesis studies have confirmed that the distal histidine in myoglobin stabilizes bound O2 by hydrogen bonding and have suggested that it is the polar character of the imidazole side chain rather than its size that limits the rate of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5da9521351e8e1c7b09172998273de1
https://doi.org/10.1021/bi00239a025
https://doi.org/10.1021/bi00239a025
Autor:
Theodore E. Carver, Ronald J. Rohlfs, Quentin H. Gibson, John S. Olson, Barry A. Springer, Richard S. Blackmore, Stephen G. Sligar
Publikováno v:
Journal of Biological Chemistry. 265:20007-20020
Time courses for NO, O2, CO, methyl and ethyl isocyanide rebinding to native and mutant sperm whale myoglobins were measured at 20 degrees C following 17-ns and 35-ps laser excitation pulses. His64 (E7) was replaced with Gly, Val, Leu, Phe, and Gln,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c0cbbe6f0e329d186c645f2dab9bccc
https://doi.org/10.1016/s0021-9258(17)45475-5
https://doi.org/10.1016/s0021-9258(17)45475-5