Results 281 to 290 of about 703,303 (322)
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Hepatology, 1969
The liver manufactures albumin at a massive rate and decreases production in times of environmental, nutritional, toxic and trauma stress. Osmotic pressure is a basic evolutionary regulatory factor, and hormonal control over albumin production has been demonstrated.
M A, Rothschild+2 more
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The liver manufactures albumin at a massive rate and decreases production in times of environmental, nutritional, toxic and trauma stress. Osmotic pressure is a basic evolutionary regulatory factor, and hormonal control over albumin production has been demonstrated.
M A, Rothschild+2 more
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Journal of Molecular Biology, 1977
We have tested the amino acid sequence of human serum albumin to check Brown's (1976) hypothesis that the molecule contains three homologous domains, of approximately 190 amino acids each, which evolved by gene duplication. A comparison of the sequence with itself shows that the repeats are extremely strong, and the probability that they could have ...
John E. Walker, A.D. McLachlan
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We have tested the amino acid sequence of human serum albumin to check Brown's (1976) hypothesis that the molecule contains three homologous domains, of approximately 190 amino acids each, which evolved by gene duplication. A comparison of the sequence with itself shows that the repeats are extremely strong, and the probability that they could have ...
John E. Walker, A.D. McLachlan
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Aldolase activity of serum albumins
Organic & Biomolecular Chemistry, 2011Bovine and human serum albumins catalyze the aldol reaction of aromatic aldehyedes and acetone, with saturation kinetics and moderate and opposite enantioselectivity. The reaction occurs at the binding site in domain IIa, and is inhibited by warfarin. Kinetic data are consistent with an enamine mechanism.
BENEDETTI, FABIO+2 more
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Serum albumin and nutritional status
Journal of Parenteral and Enteral Nutrition, 1980Serum albumin concentration is frequently used to define nutritional status. To validate this relationship, 161 body composition studies were performed on 102 patients simultaneously with protein electrophoresis. The body cell mass represented by the exchangeable potassium to total body water ratio correlated significantly (p < 0.001) with the serum
R. Armour Forse, Harry M. Shizgal
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1994
Publisher Summary This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin. The most outstanding property of albumin is its ability to bind reversibly an incredible variety of ligands.
Joseph X. Ho, Daniel C. Carter
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Publisher Summary This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin. The most outstanding property of albumin is its ability to bind reversibly an incredible variety of ligands.
Joseph X. Ho, Daniel C. Carter
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Albumin Naskapi: A New Variant of Serum Albumin
Science, 1966An apparently new variant of human serum albumin, albumin Naskapi, has been found in high frequency in the Naskapi Indians of Quebec and, in lower frequency, in other North American Indians. The family and population data of the albumin are consistent with its inheritance as a simple autosomal trait controlled by a gene designated
B. S. Blumberg, Liisa Melartin
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Differences between Urinary Albumin and Serum Albumin
Nature, 1962IN the work reported here, the molecular size and the peptide patterns of the albumins found in normal urine were compared with those of serum albumin.
Ezio Merler+3 more
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Albumin Mexico, a New Variant of Serum Albumin
Nature, 1967AN 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+3 more
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