Zobrazeno 1 - 10
of 18
pro vyhledávání: '"George C. Na"'
Publikováno v:
Pharmaceutical Research. 16:562-568
Purpose. To determine the cloud point of a variety of nonionic surfactants and to search for means to raise the surfactant cloud point in liquid formulations.
Autor:
Bacon Edward R, George C. Na, Elkan F. Halpern, Gregory L. McIntire, John Cannillo, G. Scott Gazelle, Gerald L. Wolf
Publikováno v:
Academic Radiology. 1:358-363
Rationale and Objectives. Immobility and massage produce different local limb lymph flow rates. We studied their influence on accumulation of radiopaque nanoparticulates in regional lymph nodes of normal rabbits. Methods. Quantitative lymphography at
Publikováno v:
Pharmacologytherapeutics. 52(2)
The physico-chemical methods for the study of the binding of ligands to tubulin are examined in-depth, emphasizing the assumptions on which they are based and their limitations. The criteria of specificity and linkage to protein self-association are
Autor:
Sérgio A. Mota-Rolim, Achilleas Pavlou, George C. Nascimento, John Fontenele-Araujo, Sidarta Ribeiro
Publikováno v:
Frontiers in Neuroscience, Vol 13 (2019)
Externí odkaz:
https://doaj.org/article/8cb26b098f6d4a86917731afc696a214
Publikováno v:
Biochemistry. 28:7153-7161
The in vitro fibril assembly of calf skin collagen was examined as a function of ionic strength and temperature. In a 0.03 M NaPi, pH 7.0, buffer, fibril assembly required a minimum critical concentration of collagen. At nearly physiological ionic st
Autor:
Serge N. Timasheff, George C. Na
Publikováno v:
Biochemistry. 19:1347-1354
The self-association of calf brain tubulin in PG buffer (10(-2) M NaPi and 10(-4) M GTP, pH 7.0) induced by the antimitotic drug vinblastine has been investigated by velocity sedimentation. Schlieren sedimentation patterns were examined at low vinbla
Autor:
George C. Na
Publikováno v:
Biochemistry. 28:7161-7167
Type I collagen purified from calf skin was further separated into monomeric and oligomeric fractions and characterized with gel electrophoresis and measurement of solution viscosity. The thermal stabilities of the triple-helical structure of the col
Publikováno v:
Biochemistry. 25:958-966
Glycerol inhibits the in vitro self-association of monomeric collagen into fibrils and induces the dissociation of fibrils preassembled from NaBH4-reduced collagen. These effects were investigated in an effort to understand the mechanism of fibril as
Autor:
George C. Na
Publikováno v:
Biochemistry. 25:967-973
Glycerol stabilizes the triple-helical structure of solubilized calf skin collagen. The equilibrium melting temperature of the protein increased linearly from 38.0 degrees C in AS buffer (0.01 M NaOAc and 0.02 M NaCl, pH 4.0) to 43.0 degrees C in AS
Autor:
George C. Na, Serge N. Timasheff
Publikováno v:
Biochemistry. 25:6214-6222
The binding of the anticancer drug vinblastine to calf brain tubulin was measured by a batch gel filtration method in PG buffer (0.01 M NaPi, 10(-4) M GTP, pH 7.0) at three different protein concentrations. The Scatchard binding isotherms obtained we