Results 271 to 280 of about 835,682 (316)
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On the kinetics of turnover of serum albumin
Biochimica et Biophysica Acta, 1957Abstract 1. 1. The isotope concentrations of serum albumin were determined (a) after feeding of 1- 14 C-glycine and 1- 13 C-glycine at a 5 day interval and (b) after transfusion of plasma doubly labeled with both 14 C and 13 C glycine. From the difference of the isotope concentration changes in the two animals, exchange of glycine residues in ...
N W, PENN, S, MANDELES, H S, ANKER
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Interactions of calcium with serum albumin
Archives of Biochemistry and Biophysics, 1953Abstract 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.
S, KATZ, I M, KLOTZ
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The cryoaggregation of bovine serum albumin
Cryobiology, 1970Summary 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
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Serum albumin in pig epididymis
Comparative Biochemistry and Physiology, 19681. 1. The proteins of the fluid of the tail of the epididymis (ETF) in boars (Sus scrofa ferus—forma domestica males) were compared with serum proteins by means of acrylamide gel electrophoresis. 2. 2. In ETF a fraction was found which corresponded in its mobility to serum albumin. 3. 3.
E, Sedláková, J, Dostál, J, Matousek
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Redox properties of serum albumin
Biochimica et Biophysica Acta (BBA) - General Subjects, 2013Oxidative damage results in protein modification, and is observed in numerous diseases. Human serum albumin (HSA), the most abundant circulating protein in the plasma, exerts important antioxidant activities against oxidative damage.The present review focuses on the characterization of chemical changes in HSA that are induced by oxidative damage, their
Anraku, M. +3 more
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Preparation of Serum Albumin Microcapsules
Journal of Pharmaceutical Sciences, 1985Simple coacervation of bovine serum albumin was studied to prepare biodegradable microcapsules. Three types of microcapsules, which differed in shape, were obtained by changing either core size or the bovine serum albumin concentrations of the coacervating systems.
T, Ishizaka +3 more
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Species specificity in serum albumins
Comparative Biochemistry and Physiology, 1963Abstract 1. 1. The serum albumins of six mammalian species have been studied by methods which permit comparison of their primary structure. 2. 2. Chromatograms of the peptides produced by tryptic digestion of performate-oxidized proteins revealed patterns indicating major species differences. 3. 3.
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Site of Catabolism of Serum Albumin
Nature, 1958THE 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.
D, GITLIN, J R, KLINENBERG, W L, HUGHES
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The interaction of serum albumin with ethanol
Archives of Biochemistry and Biophysics, 1962Abstract 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
R M, ROSENBERG +3 more
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The heterogeneity of bovine serum albumin
Biochimica et Biophysica Acta (BBA) - General Subjects, 1966Abstract 1. 1. The different components of native and modified bovine serum albumin have been investigated with respect to differences in composition and structure. It was found that native bovine serum albumin is composed of at least 3 components, and that most bovine serum albumin samples contain 4.
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