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Human serum albumin
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<h2 id="function">Function</h2> <ul><li>Maintains <a href="/facts/Oncotic_pressure/d1YAUqmF">oncotic pressure</a></li> <li>Transports <a href="/facts/Thyroid_hormone/9k4xJtCq">thyroid hormones</a></li> <li>Transports other hormones, in particular, ones that are fat-soluble</li> <li>Transports <a href="/facts/Fatty_acids/JGg3erIu">fatty acids</a> ("free" fatty acids) to the liver and to myocytes for utilization of energy</li> <li>Transports unconjugated <a href="/facts/Bilirubin/HCHyCjkt">bilirubin</a></li> <li>Transports many <a href="/facts/Medication/h9mhwWP2">drugs</a>; serum albumin levels can affect the half-life of drugs. Competition between drugs for albumin binding sites may cause drug interaction by increasing the free fraction of one of the drugs, thereby affecting potency.</li> <li>Competitively binds <a href="/facts/Calcium/hf252CC0">calcium</a> ions (Ca2+)</li> <li>Serum albumin, as a negative acute-phase protein, is down-regulated in inflammatory states. As such, it is not a valid marker of nutritional status; rather, it is a marker of an inflammatory state</li> <li>Prevents photodegradation of <a href="/facts/Folic_acid/8Eb7An6D">folic acid</a></li> <li>Prevent pathogenic effects of <i><a href="/facts/Clostridioides_difficile_infection/kYFGjVKf">Clostridioides difficile</a></i> toxins<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a></li></ul> <h2 id="measurement">Measurement</h2> <p>Serum albumin is commonly measured by recording the change in <a href="/facts/Absorbance/Rnv6VMX1">absorbance</a> upon binding to a dye such as <a href="/facts/Bromocresol_green/7EB9ufYo">bromocresol green</a> or <a href="/facts/Bromocresol_purple/2GlMKSyq">bromocresol purple</a>.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> </p> <h2 id="reference-ranges">Reference ranges</h2> <p>The normal range of human serum albumin in adults (> 3 y.o.) is 3.5–5.0 g/dL (35–50 g/L). For children less than three years of age, the normal range is broader, 2.9–5.5 g/dL.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p><p>Low albumin (<a href="/facts/Hypoalbuminemia/sJD2mV5w">hypoalbuminemia</a>) may be caused by <a href="/facts/Liver_disease/NHtuS0gU">liver disease</a>, <a href="/facts/Nephrotic_syndrome/YG7bUzWV">nephrotic syndrome</a>, burns, <a href="/facts/Protein-losing_enteropathy/BdreWjR0">protein-losing enteropathy</a>, <a href="/facts/Malabsorption/hWRQd4c5">malabsorption</a>, <a href="/facts/Malnutrition/KasQy5MR">malnutrition</a>, late pregnancy, artefact, genetic variations and malignancy. </p><p>High albumin (<a href="/facts/Hyperalbuminemia/wI8vu5py">hyperalbuminemia</a>) is almost always caused by dehydration. In some cases of <a href="/facts/Retinol/pUwofb2S">retinol</a> (<a href="/facts/Vitamin_A/5ewDf9LF">Vitamin A</a>) deficiency, the albumin level can be elevated to high-normal values (e.g., 4.9 g/dL) because retinol causes cells to swell with water. (This is also the reason too much Vitamin A is toxic.)<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> This swelling also likely occurs during treatment with 13-cis retinoic acid (<a href="/facts/Isotretinoin/XBKv4fQJ">isotretinoin</a>), a pharmaceutical for treating severe acne, amongst other conditions. In lab experiments it has been shown that all-trans retinoic acid down regulates human albumin production.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> </p> <h2 id="pathology">Pathology</h2> <h3>Hypoalbuminemia</h3> <p><a href="/facts/Hypoalbuminemia/sJD2mV5w">Hypoalbuminemia</a> means low blood albumin levels.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> This can be caused by: </p> <ul><li><a href="/facts/Liver_disease/NHtuS0gU">Liver disease</a>; <a href="/facts/Cirrhosis/bkLuLvCD">cirrhosis</a> of the liver is most common</li> <li>Excess excretion by the <a href="/facts/Kidneys/HBspPrv9">kidneys</a> (as in <a href="/facts/Nephrotic_syndrome/YG7bUzWV">nephrotic syndrome</a>)</li> <li>Excess loss in bowel (protein-losing enteropathy, e.g., <a href="/facts/M%C3%A9n%C3%A9trier%27s_disease/QzJ3yGFo">Ménétrier's disease</a>)</li> <li>Burns (plasma loss in the absence of skin barrier)</li> <li>Redistribution (hemodilution [as in <a href="/facts/Pregnancy/vEKYGpep">pregnancy</a>], increased vascular permeability or decreased lymphatic clearance)</li> <li>Acute disease states (referred to as a negative <a href="/facts/Acute-phase_protein/QkeAFAk5">acute-phase protein</a>)<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a></li> <li><a href="/facts/Malnutrition/KasQy5MR">Malnutrition</a> and wasting<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a></li> <li>Mutation causing analbuminemia (very rare)</li> <li><a href="/facts/Anorexia_nervosa/00KSqEn7">Anorexia nervosa</a> (most common cause in adolescents)</li></ul> <p>In clinical medicine, hypoalbuminemia significantly correlates with a higher mortality rates in several conditions such as heart failure, post-surgery, COVID-19.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> </p> <h3>Hyperalbuminemia</h3> <p>Hyperalbuminemia is an increased concentration of albumin in the blood.<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> Typically, this condition is due to dehydration.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> Hyperalbuminemia has also been associated with high protein diets.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> </p> <h3>Medical use</h3> <p>Human albumin solution (HSA) is available for medical use, usually at concentrations of either 5 or 25%. </p><p>Human albumin is often used to replace lost fluid and help restore blood volume in trauma, burns and surgery patients. There is no strong medical evidence that albumin administration (compared to saline) saves lives for people who have <a href="/facts/Hypovolemia/MmP8TsPw">hypovolaemia</a> or for those who are critically ill due to burns or <a href="/facts/Hypoalbuminemia/sJD2mV5w">hypoalbuminaemia</a>.<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> It is also not known if there are people who are critically ill that may benefit from albumin.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> Therefore, the <a href="/facts/Cochrane_Collaboration/UlmdJ1H8">Cochrane Collaboration</a> recommends that it should not be used, except in <a href="/facts/Clinical_trials/q8LMr832">clinical trials</a>.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a><a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> </p><p>In <a href="/facts/Acoustic_droplet_vaporization/GkNH2ISl">acoustic droplet vaporization</a> (ADV), albumin is sometimes used as a <a href="/facts/Surfactant/zgVX6g8o">surfactant</a>. ADV has been proposed as a cancer treatment by means of occlusion therapy.<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> </p><p>Human serum albumin may be used to potentially reverse drug/chemical toxicity by binding to free drug/agent.<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> </p><p>Human albumin may also be used in treatment of decompensated cirrhosis.<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> </p><p>Human serum albumin has been used as a component of a <a href="/facts/Frailty_syndrome/T1Mho2tf">frailty</a> index.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a> </p> <h2 id="glycation">Glycation</h2> <p>It has been known for a long time that human blood proteins like hemoglobin<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> and serum albumin<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a><a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a> may undergo a slow non-enzymatic <a href="/facts/Glycation/3CHvekIg">glycation</a>, mainly by formation of a Schiff base between ε-amino groups of lysine (and sometimes arginine) residues and glucose molecules in blood (<a href="/facts/Maillard_reaction/7vtYtpGk">Maillard reaction</a>). This reaction can be inhibited in the presence of antioxidant agents.<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> Although this reaction may happen normally,<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> elevated glycoalbumin is observed in diabetes mellitus.<a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a> </p><p>Glycation has the potential to alter the biological structure and function of the serum albumin protein.<a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a><a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a><a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a><a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a> </p><p>Moreover, the glycation can result in the formation of Advanced Glycation End-Products (AGE), which result in abnormal biological effects. Accumulation of AGEs leads to tissue damage via alteration of the structures and functions of tissue proteins, stimulation of cellular responses, through receptors specific for AGE-proteins, and generation of reactive oxygen intermediates. AGEs also react with DNA, thus causing mutations and DNA transposition. Thermal processing of proteins and carbohydrates brings major changes in allergenicity. AGEs are antigenic and represent many of the important neoantigens found in cooked or stored foods.<a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a> They also interfere with the normal product of nitric oxide in cells.<a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a> </p><p>Although there are several lysine and arginine residues in the serum albumin structure, very few of them can take part in the glycation reaction.<a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a><a class="footnote-ref" id="fnref:39" href="#fn:39"><sup>39</sup></a> </p> <h2 id="oxidation">Oxidation</h2> <p>The albumin is the predominant protein in most body fluids, its Cys34 represents the largest fraction of free thiols within the body. The albumin Cys34 thiol exists in both reduced and oxidized forms.<a class="footnote-ref" id="fnref:40" href="#fn:40"><sup>40</sup></a> In plasma of healthy young adults, 70–80% of total HSA contains the free sulfhydryl group of Cys34 in a reduced form or mercaptoalbumin (HSA-SH).<a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a> However, in pathological states characterized by oxidative stress such as kidney disease, liver disease and diabetes the oxidized form, or non-mercaptoalbumin (HNA), could predominate.<a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a><a class="footnote-ref" id="fnref:43" href="#fn:43"><sup>43</sup></a> The albumin thiol reacts with radical hydroxyl (.OH), hydrogen peroxide (H2O2) and the reactive nitrogen species as peroxynitrite (ONOO.), and have been shown to oxidize Cys34 to sulfenic acid derivate (HSA-SOH), it can be recycled to mercapto-albumin; however at high concentrations of reactive species leads to the irreversible oxidation to sulfinic (HSA-SO2H) or sulfonic acid (HSA-SO3H) affecting its structure.<a class="footnote-ref" id="fnref:44" href="#fn:44"><sup>44</sup></a> Presence of reactive oxygen species (ROS), can induce irreversible structural damage and alter protein activities. </p> <h2 id="loss-via-kidneys">Loss via kidneys</h2> <p>In the healthy <a href="/facts/Kidney/HBspPrv9">kidney</a>, albumin's size and negative electric charge exclude it from excretion in the <a href="/facts/Glomerulus/C7VsNqPJ">glomerulus</a>. This is not always the case, as in some <a href="/facts/Kidney_diseases/koq79A75">diseases</a> including <a href="/facts/Diabetic_nephropathy/GHmG7ofQ">diabetic nephropathy</a>, which can sometimes be a complication of uncontrolled or of longer term <a href="/facts/Diabetes/2xeHXbsI">diabetes</a> in which proteins can cross the glomerulus. The lost albumin can be detected by a simple urine test.<a class="footnote-ref" id="fnref:45" href="#fn:45"><sup>45</sup></a> Depending on the amount of albumin lost, a patient may have normal renal function, <a href="/facts/Microalbuminuria/9BNNAEWd">microalbuminuria</a>, or <a href="/facts/Albuminuria/pXvBqGqh">albuminuria</a>. </p> <h2 id="interactions">Interactions</h2> <p>Human serum albumin has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with <a href="/facts/FCGRT/stas5uDh">FCGRT</a>.<a class="footnote-ref" id="fnref:46" href="#fn:46"><sup>46</sup></a> </p><p>It might also interact with a yet-unidentified <a href="/facts/Albondin/nHnorrhR">albondin</a> (gp60), a certain pair of gp18/gp30, and some other proteins like <a href="/facts/Osteonectin/uwKjq5XD">osteonectin</a>, <a href="/facts/Heterogeneous_ribonucleoprotein_particle/YrbVK8r9">hnRNPs</a>, <a href="/facts/Calreticulin/gBGh7vLu">calreticulin</a>, <a href="/facts/Cubilin/5EgLmpWI">cubilin</a>, and <a href="/facts/Megalin/dxfbGQGm">megalin</a>.<a class="footnote-ref" id="fnref:47" href="#fn:47"><sup>47</sup></a> </p> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Bovine_serum_albumin/forQfk4f">Bovine serum albumin</a></li> <li><a href="/facts/Serum_albumin/KW1YhuF3">Serum albumin</a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Komatsu T, Nakagawa A, Curry S, Tsuchida E, Murata K, Nakamura N, Ohno H (September 2009). "The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O(2) and CO binding to iron protoporphyrin IX". <i>Organic & Biomolecular Chemistry</i>. 7 (18): 3836–3841. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1039%2Fb909794e">10.1039/b909794e</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19707690">19707690</a>.</li> <li>Milojevic J, Raditsis A, Melacini G (November 2009). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770600">"Human serum albumin inhibits Abeta fibrillization through a "monomer-competitor" mechanism"</a>. <i>Biophysical Journal</i>. 97 (9): 2585–2594. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2009BpJ....97.2585M">2009BpJ....97.2585M</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.bpj.2009.08.028">10.1016/j.bpj.2009.08.028</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770600">2770600</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19883602">19883602</a>.</li> <li>Silva AM, Hider RC (October 2009). "Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron. Implications for non-transferrin-bound iron speciation". <i>Biochimica et Biophysica Acta</i>. 1794 (10): 1449–1458. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.bbapap.2009.06.003">10.1016/j.bbapap.2009.06.003</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19505594">19505594</a>.</li> <li>Otosu T, Nishimoto E, Yamashita S (February 2010). "Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy". <i>Journal of Biochemistry</i>. 147 (2): 191–200. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fjb%2Fmvp175">10.1093/jb/mvp175</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19884191">19884191</a>.</li> <li>Blindauer CA, Harvey I, Bunyan KE, Stewart AJ, Sleep D, Harrison DJ, et al. (August 2009). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755717">"Structure, properties, and engineering of the major zinc binding site on human albumin"</a>. <i>The Journal of Biological Chemistry</i>. 284 (34): 23116–23124. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M109.003459">10.1074/jbc.M109.003459</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755717">2755717</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19520864">19520864</a>.</li> <li>Juárez J, López SG, Cambón A, Taboada P, Mosquera V (July 2009). "Influence of electrostatic interactions on the fibrillation process of human serum albumin". <i>The Journal of Physical Chemistry B</i>. 113 (30): 10521–10529. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1021%2Fjp902224d">10.1021/jp902224d</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19572666">19572666</a>.</li> <li>Fu BL, Guo ZJ, Tian JW, Liu ZQ, Cao W (August 2009). "[Advanced glycation end products induce expression of PAI-1 in cultured human proximal tubular epithelial cells through NADPH oxidase dependent pathway]". <i>Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi = Chinese Journal of Cellular and Molecular Immunology</i>. 25 (8): 674–677. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19664386">19664386</a>.</li> <li>Ascenzi P, di Masi A, Coletta M, Ciaccio C, Fanali G, Nicoletti FP, et al. (November 2009). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2781501">"Ibuprofen impairs allosterically peroxynitrite isomerization by ferric human serum heme-albumin"</a>. <i>The Journal of Biological Chemistry</i>. 284 (45): 31006–31017. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M109.010736">10.1074/jbc.M109.010736</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2781501">2781501</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19734142">19734142</a>.</li> <li>Sowa ME, Bennett EJ, Gygi SP, Harper JW (July 2009). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2716422">"Defining the human deubiquitinating enzyme interaction landscape"</a>. <i>Cell</i>. 138 (2): 389–403. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.cell.2009.04.042">10.1016/j.cell.2009.04.042</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2716422">2716422</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19615732">19615732</a>.</li> <li>Curry S (August 2002). <a href="https://doi.org/10.1111%2Fj.1423-0410.2002.tb05326.x">"Beyond expansion: structural studies on the transport roles of human serum albumin"</a>. <i>Vox Sanguinis</i>. 83 (Suppl 1): 315–319. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1111%2Fj.1423-0410.2002.tb05326.x">10.1111/j.1423-0410.2002.tb05326.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12617161">12617161</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:44482133">44482133</a>.</li> <li>Guo S, Shi X, Yang F, Chen L, Meehan EJ, Bian C, Huang M (September 2009). "Structural basis of transport of lysophospholipids by human serum albumin". <i>The Biochemical Journal</i>. 423 (1): 23–30. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1042%2FBJ20090913">10.1042/BJ20090913</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19601929">19601929</a>.</li> <li>de Jong PE, Gansevoort RT (2009). <a href="https://doi.org/10.1159%2F000201568">"Focus on microalbuminuria to improve cardiac and renal protection"</a>. <i>Nephron Clinical Practice</i>. 111 (3): c204-10, discussion c211. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1159%2F000201568">10.1159/000201568</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19212124">19212124</a>.</li> <li>Page TA, Kraut ND, Page PM, Baker GA, Bright FV (September 2009). "Dynamics of loop 1 of domain I in human serum albumin when dissolved in ionic liquids". <i>The Journal of Physical Chemistry B</i>. 113 (38): 12825–12830. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1021%2Fjp904475v">10.1021/jp904475v</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19711930">19711930</a>.</li> <li>Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E (June 2008). <a href="https://doi.org/10.1016%2Fj.febslet.2008.04.057">"The antioxidant properties of serum albumin"</a>. <i>FEBS Letters</i>. 582 (13): 1783–1787. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.febslet.2008.04.057">10.1016/j.febslet.2008.04.057</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/18474236">18474236</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:5364683">5364683</a>.</li> <li>Wyatt AR, Wilson MR (February 2010). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2823492">"Identification of human plasma proteins as major clients for the extracellular chaperone clusterin"</a>. <i>The Journal of Biological Chemistry</i>. 285 (6): 3532–3539. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M109.079566">10.1074/jbc.M109.079566</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2823492">2823492</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/19996109">19996109</a>.</li> <li>Cui FL, Yan YH, Zhang QZ, Qu GR, Du J, Yao XJ (February 2010). 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