Results 341 to 350 of about 3,192,320 (388)

Bovine Serum Albumin as a Versatile Platform for Cancer Imaging and Therapy.

Current Medicinal Chemistry, 2018
BACKGROUND Due to the good biocompatibility, biodegradability, facile surface functionalization and high water solubility, Bovine serum albumin has gain increasing attention in the nanomedicine. OBJECTIVE Despite there are many reviews on albumin based
Jun Wang, Bingbo Zhang
semanticscholar   +1 more source

Novel Chlorinated Polyfluorinated Ether Sulfonates and Legacy Per-/Polyfluoroalkyl Substances: Placental Transfer and Relationship with Serum Albumin and Glomerular Filtration Rate.

Environmental Science and Technology, 2017
Per- and polyfluoroalkyl substances (PFASs) may cross the placental barrier and lead to fetal exposure. However, little is known about the factors that influence maternal-fetal transfer of these chemicals.
Yitao Pan, Yingshuang Zhu, T. Zheng, Qianqian Cui, S. Buka, Bin Zhang, Yong Guo, W. Xia, L. Yeung, Yuan-yuan Li, Aifen Zhou, Lin Qiu, Hongxiu Liu, Minmin Jiang, Chuansha Wu, Shunqing Xu, Jiayin Dai   +16 more
semanticscholar   +1 more source

Albumin Mexico, a New Variant of Serum Albumin

Nature, 1967
AN inherited variant of albumin (albumin Naskapi) has recently been described which has an electrophoretic mobility greater than that of common albumin (albumin A)1. This variant is relatively common in many North American Indian tribes, but it has not been found in the United States white and negro sera so far tested, nor in many European sera.
Baruch S. Blumberg, Rubén Lisker, Liisa Melartin, Liisa Melartin   +3 more
openaire   +3 more sources

On the biosynthesis of serum albumin

Trends in Biochemical Sciences, 1976
Abstract The intracellular biosynthetic precursor of albumin in the plasma is a proalbumin containing a highly basic N-terminal hexapeptide. Analogies with other secreted proteins raise some interesting problems.
P.S. Quinn, J.D. Judah
openaire   +2 more sources

Site of Catabolism of Serum Albumin

Nature, 1958
THE relative importance of the liver, kidneys and intestines for the catabolism of serum albumin has been examined in Swiss albino mice, 5–6 weeks of age. Mouse serum albumin and human serum albumin were labelled with iodine-131 as described elsewhere1 and given to the mice intravenously, about 0.5 µc or 5–15 µgm. iodoalbumin per mouse.
Walter L. Hughes, James R. Klinenberg, David Gitlin, David Gitlin   +3 more
openaire   +3 more sources

Catalytic properties of serum albumin

Pharmacological Research Communications, 1983
In this work it has been observed that human blood plasma is able to catalyse the reaction between tert.butyl hydroperoxide and 2-nitro-5-mercaptobenzoic acid. The purification of a proteic fraction responsible for this activity indicated it is due to plasma albumin; this is also demonstrated using various purified commercial albumins.
M.G. Banchelli, Franca Buffoni, G. Ignesti, Laura Raimondi, Renato Pirisino   +4 more
openaire   +3 more sources

The interaction of serum albumin with ethanol

Archives of Biochemistry and Biophysics, 1962
Abstract The reduced viscosity and specific rotation of 1% solutions of bovine serum albumin in aqueous ethanol were obtained at pH's 2, 3, and 4 at low ionic strength, and at high salt concentration at the isoionic point. The data are consistent with increased helical content and the breaking of hydrophobic bonds as a result of adding ethanol at low
Jon E. Haebig, Jon E. Haebig, Donald W. Rogers, Donald W. Rogers, Robert M. Rosenberg, Robert M. Rosenberg, Theodore L. Steck, Theodore L. Steck   +7 more
openaire   +3 more sources

No Serum Albumin in Myeloma [PDF]

Archives of Internal Medicine, 1991
To the Editor.—— Chen and Magalhaes1recently showed an inverse correlation between serum albumin and paraprotein concentrations in patients with IgG multiple myeloma, but not in patients with IgA or light-chain myeloma. In exploring the implications of this relationship, several possibilities come to mind. First, the low albumin level might be due to
openaire   +1 more source

Interactions of calcium with serum albumin

Archives of Biochemistry and Biophysics, 1953
Abstract Binding of calcium ions by bovine serum albumin has been found to be essentially independent of temperature over the range 0 to 25 °C. On the other hand, pH has a very pronounced effect. No complexes with calcium are detectable until the protein is appreciably above its isoelectric point.
Sam Katz, Irving M. Klotz
openaire   +3 more sources

The cryoaggregation of bovine serum albumin

Cryobiology, 1970
Summary Bovine serum albumin in the native (BSA), reduced (BSA-SH), and combined (BSA-S-NEM) forms was frozen at −5°C. The BSA remained essentially soluble; the BSA-SH and BSA-S-NEM both aggregated nearly completely when allowed to reimbibe water at room temperature but to a smaller degree when allowed to reimbibe just above the freezing point.
R. Goodin, J. Levitt
openaire   +3 more sources