1970
DOI: 10.1016/s0026-0495(70)90236-2
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Distribution of protein-bound zinc in normal and cirrhotic serum

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Cited by 88 publications
(23 citation statements)
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“…Several hypotheses have been put forward to explain why the serum concentration of zinc decreases with development of liver disease: First, zinc exists in the blood, where one-third of it is bound to α 2 -macroglobulin and the rest is bound to albumin. The serum concentration of zinc consequently decreases with decreases in the albumin concentration as the liver disease develops [18,19]. Second, when a shunt between the portal vein and the systemic circulation is enlarged with development of disease, the amount of zinc excreted into the urine increases, and as a result, the serum zinc concentration decreases [20].…”
Section: Discussionmentioning
confidence: 99%
“…Several hypotheses have been put forward to explain why the serum concentration of zinc decreases with development of liver disease: First, zinc exists in the blood, where one-third of it is bound to α 2 -macroglobulin and the rest is bound to albumin. The serum concentration of zinc consequently decreases with decreases in the albumin concentration as the liver disease develops [18,19]. Second, when a shunt between the portal vein and the systemic circulation is enlarged with development of disease, the amount of zinc excreted into the urine increases, and as a result, the serum zinc concentration decreases [20].…”
Section: Discussionmentioning
confidence: 99%
“…The complex formation equilibria (stoichiometry and stability constants) for the parent systems are known in the literature under our selected experimental conditions in almost all cases [17,22,23]. However, serum proteins can also bind considerable amounts of zinc(II) or its complexes [24,25]. The hypothesis is widely held that circulating zinc is transported mainly by albumin, and that transferrin is the carrier of newly absorbed zinc in the portal plasma [24].…”
Section: Introductionmentioning
confidence: 99%
“…The binding site is situated at the interface of domains I and II, which consists of two Hisnitrogen atoms (His-67, His-247), two carboxylate-oxygen donor atoms (Asn-99, Asp-249) and a water molecule in the coordination sphere, and the Zn center adopts a distorted trigonal bipyramidal geometry [26,34]. a2M is a fairly large protein with 720 kDa, but found at much lower concentration in the blood than albumin (2-6 mM), and with conditional formation constants of logK 1 ' 5 7.49 and logK 2 ' 5 5.12 it has also considerable Zn(II)-binding properties [29,[35][36][37]. Another possible Zn(II) binder is the 79 kDa iron transport protein Tf (37 mM in serum), but 30% of the binding sites are occupied by Fe(III) ions in the serum [27,33].…”
Section: Resultsmentioning
confidence: 99%
“…Literature data show that most of the total serum Zn(II) is bound to the serum proteins (appr. 98%) and HSA is the primary target (80-90%) [32,35,37], followed by a2M (5-15%) [35][36][37]. However, the role of Tf is under discussion [36,38] and also a minority of Zn(II) is circulating unbound or attached to LMM components (considered as the mobile portion of the metal ion).…”
Section: Resultsmentioning
confidence: 99%