Topic
Serum albumin
About: Serum albumin is a research topic. Over the lifetime, 16337 publications have been published within this topic receiving 516395 citations. The topic is also known as: blood albumin & ANALBA.
Papers published on a yearly basis
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TL;DR: Despite the probable importance of the free thyroid hormone, few reports have dealt with its measurement in the plasma and the absolute concentration of free hormone in serum cannot be calculated from such methods.
Abstract: There exists a great deal of evidence that it is the free or unbound portion of the circulating thyroid hormone that is accessible to the tissues and physiologically active, whereas the great majority of the hormone, which is protein bound, serves as a metabolically inert reservoir (1-4). If this is the case, then the concentration of free hormone in the plasma must be a major determinant of both the metabolic effectiveness and the rate of removal of the thyroid hormone in the blood. Despite the probable importance of the free thyroid hormone, few reports have dealt with its measurement in the plasma. Certain methods for directly measuring the proportion of free thyroxine (T4) in serum appear to have either technical or theoretical disadvantages (5, 6), although others have not been completely evaluated (7). On the other hand, there has been described a variety of methods, such as in vitro red blood cell or resin uptake techniques, which reflect the proportion of free thyroid hormone in the serum, but do not directly measure this function (8-11). Consequently, the absolute concentration of free hormone in serum cannot be calculated from such re-
170 citations
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TL;DR: The agreement between the results obtained with these independent techniques adds some confidence to the use of the [14C]leucine method and is suggested that the stimulus for increased secretion is a small increase in the quantity of albumin in the microsomal particles.
170 citations
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169 citations
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169 citations
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TL;DR: Structural-based modelling of the FcRn–albumin complex is presented, supported by binding analysis of site-specific mutants, providing mechanistic evidence for the presence of pH-sensitive ionic networks at the interaction interface.
Abstract: Albumin transport proteins circulate in the blood and are protected from degradation by interaction with the neonatal Fc receptor. Andersen et al. investigate the albumin binding site of the neonatal Fc receptor and find pH sensitive ionic networks at the binding interface.
169 citations