Results 291 to 300 of about 703,303 (322)
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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.
Walter L. Hughes +3 more
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Catalytic properties of serum albumin
Pharmacological Research Communications, 1983In 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 +4 more
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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
Jon E. Haebig +7 more
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On the biosynthesis of serum albumin
Trends in Biochemical Sciences, 1976Abstract 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
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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
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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.
Sam Katz, Irving 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.
J. Dostál +2 more
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The Measurement of Albumin in Serum and Plasma [PDF]
Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 1985 This publication was prepared at the invitation of the Analytical Methods Working Party of the Scientific Committee of the Association of Clinical Biochemists, but does not necessarily reflect the views of the Scientific Committee.
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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.
Masumi Koishi +3 more
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