Albumin: Structure, Function and Uses 1977
DOI: 10.1016/b978-0-08-019603-9.50010-7
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Some Aspects of the Structure and Conformational Properties of Serum Albumin

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Cited by 148 publications
(110 citation statements)
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“…This behaviour is consistent with previous descriptions of the N to B transition as involving a subtle isomerisation, such as a rearrangement of subdomaidsubdomain or domaiddomain contacts [12], with little change in helical content (51 -48%) [12].…”
Section: Other Resonancessupporting
confidence: 92%
See 1 more Smart Citation
“…This behaviour is consistent with previous descriptions of the N to B transition as involving a subtle isomerisation, such as a rearrangement of subdomaidsubdomain or domaiddomain contacts [12], with little change in helical content (51 -48%) [12].…”
Section: Other Resonancessupporting
confidence: 92%
“…This transition may therefore involve only an increased separation of the domains, i. e. from the compact heart shape seen in crystals of HSA [19] to a linear bead form, with unfolding being confined largely to the loss of inter-domain and/or subdomain contacts and disruption of structure in the hinge or link regions. It is known from studies of optical rotation that the helical content changes very little during this transition (approximately 44-35%) [12], but there is a sharp increase in intrinsic viscosity, a more than doubling of the hydrodynamic axial ratio [20] and a 66% increase in the length of the protein [2].…”
Section: Other Resonancesmentioning
confidence: 99%
“…In this investigation, we showed, to our knowledge, in the first time that BSA did have the capacity to induce gametes adhesion and fusion in vitro. Previous study indicated that BSA conformation could change in different pH value [18]. Our result showed that the frequency of gamete adhesion and fusion decreased with the decrease of pH value (Fig.…”
Section: Discussionsupporting
confidence: 53%
“…Some studies have been performed at non-physiological temperatures (8,27), or in the absence of calcium (24)(25)(26)(27)(28)(29). Decreases in calcium concentration below physiological levels alter the conformation of albumin near physiological pH (30) and may affect its binding properties. Thirdly, structural and kinetic information can be obtained from NMR spectra, such as the relative occupation of individual binding sites on albumin, lipoproteins, and model membranes, the ionization states of fatty acids bound to each site, and estimates ofthe exchange rates of fatty acids between albumin and nonalbumin binding sites (3, 4, 1 1).…”
Section: Discussionmentioning
confidence: 99%