PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3759334-4 1986 Refolding under reducing conditions almost completely inhibited the regeneration of hydrophobic binding regions, suggesting that the formation of disulfide bonds plays an important role in the refolding of serum albumin. Disulfides 146-155 albumin Homo sapiens 206-219 3255377-0 1988 Effect of oxidative sulfitolysis of disulfide bonds of bovine serum albumin on its structural properties: a physiochemical study. Disulfides 36-45 albumin Homo sapiens 62-75 3021167-9 1986 A model is proposed wherein DSF and serum albumin rapidly form a noncovalent adduct and, subsequently, in a slow unimolecular process, DSF is reduced to one mole of free DDC and one mole of the serum albumin-DDC mixed disulfide. Disulfides 218-227 albumin Homo sapiens 36-49 3021167-9 1986 A model is proposed wherein DSF and serum albumin rapidly form a noncovalent adduct and, subsequently, in a slow unimolecular process, DSF is reduced to one mole of free DDC and one mole of the serum albumin-DDC mixed disulfide. Disulfides 218-227 albumin Homo sapiens 194-207 6609141-8 1984 The radiation-induced broadening of the serum albumin peak is interpreted as being a result of intramolecular disulfide exchange. Disulfides 110-119 albumin Homo sapiens 40-53 3896577-6 1985 Fragmentation occurs by proteolysis of the albumin molecule both at sites within and outside disulfide loops. Disulfides 93-102 albumin Homo sapiens 43-50 3896577-7 1985 The predominant cleavage site appears to be approximately two-fifths of the distance from one end of the albumin molecule to produce disulfide-linked fragments of about 45 000 and 30 000 molecular weight. Disulfides 133-142 albumin Homo sapiens 105-112 5387562-0 1969 Reduction and reoxidation of the disulfide bonds of bovine serum albumin. Disulfides 33-42 albumin Homo sapiens 59-72 6614484-1 1983 After precipitation of proteins; serum, hepatocytes, or glutathione-derivatized bovine serum albumin, by perchloric acid, dithiothreitol was used to reduce glutathione-protein mixed disulfides in the ether-washed, resuspended pellet. Disulfides 182-192 albumin Homo sapiens 87-100 920499-0 1977 On the introduction of disulfide crosslinks into fibrous proteins and bovine serum albumin. Disulfides 23-32 albumin Homo sapiens 77-90 1096943-9 1975 When bovine serum albumin was coupled to palmityl-aminoethylamino-agarose and digested with trypsin, two fragments were obtained: (a) peptide 115-184, containing the highly aromatic disulfide loop 3 of Brown"s model, and (b) a larger fragment, residues 377-581, containing disulfide loops 7-9. Disulfides 182-191 albumin Homo sapiens 12-25 237269-5 1975 The effect of calcium on Brdicka currents of bovine serum albumin in the absence of urea is attributed to an orientation of the protein on the surface of the electrode such that all disulfide groups are reduced and with other ligands can complex with Co(ii). Disulfides 182-191 albumin Homo sapiens 58-65 20285166-0 1947 The relationship of sulfhydryl and disulfide groups to the antigenic power of bovine serum albumin. Disulfides 35-44 albumin Homo sapiens 85-98 14292170-2 1965 EFFECT OF HEAT DENATURATION OF BOVINE SERUM ALBUMIN (BSA) ON SULFHYDRYL AND REACTIVE DISULFIDE CONTENT. Disulfides 85-94 albumin Homo sapiens 38-51 14057350-1 1963 The tyrosyl groups of reduced and carboxymethylated human serum albumin, in which all disulfide bonds are broken, ionize at lower pH than those of native albumin, in spite of the greater negative charge on the protein produced by the S-carboxy-methyl groups. Disulfides 86-95 albumin Homo sapiens 58-71 13628588-0 1958 [Accessibility of disulfide groups of bovine serum albumin]. Disulfides 18-27 albumin Homo sapiens 51-58 33974730-5 2021 Native mass spectrometry experiments show that the prochelators form stable disulfide conjugates with bovine serum albumin, thus affording novel bioconjugate prochelator systems. Disulfides 76-85 albumin Homo sapiens 109-122 34041901-5 2021 Hybrid albumin nanoparticles were assembled via the disulfide reprogramming method and encapsulated paclitaxel (PTX) to formulate PSN-HSA-PTX-IR780. Disulfides 52-61 albumin Homo sapiens 7-14 33515755-1 2021 Human serum albumin (HSA) contains 17 disulfides and only one reduced cysteine, Cys34, which can be oxidized to a relatively stable sulfenic acid (HSA-SOH). Disulfides 38-48 albumin Homo sapiens 6-19 33714740-0 2021 Crosslinking of human plasma C-reactive protein to human serum albumin via disulfide bond oxidation. Disulfides 75-84 albumin Homo sapiens 63-70 33714740-6 2021 Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA). Disulfides 112-121 albumin Homo sapiens 267-280 33714740-6 2021 Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA). Disulfides 231-240 albumin Homo sapiens 267-280 33855279-2 2021 Herein, we developed an in vitro system for directly monitoring PDI- or ERp46-catalyzed disulfide bond formation in ribosome-associated nascent chains of human serum albumin. Disulfides 88-97 albumin Homo sapiens 160-173 33454336-4 2021 Limited reduction of disulfide bonds resulted in non-covalent aggregation of bovine serum albumin and cleavage of only inter-chain linkages of an antibody that had no effects on its overall structure. Disulfides 21-30 albumin Homo sapiens 84-97 33446738-2 2021 Here we have found that some AMPs, such as TP4 from fish tilapia, and drugs, such as antipyretic ibuprofen, were bound by bovine serum albumin only in complex with alpha1-antitrypsin which is linked by disulfide bond. Disulfides 202-211 albumin Homo sapiens 129-142 32971812-4 2020 The data from the molten globule-like structures of ribonuclease, lysozyme, bovine serum albumin and chymotrypsinogen identified new speeding agents, i.e., hydrophobic/electrostatic interactions and productive complex formations involving the protein and thiol reagent, which were able to confer exceptional reactivity to structural cysteines which were only intended to form disulfides. Disulfides 376-386 albumin Homo sapiens 83-96 32392042-5 2020 Anti-human serum albumin pAbF antibody was modified with azide groups and conjugated to UCNP@PEG-alkyne via click reaction; alternatively, the antibody, after mild reduction of its disulfide bonds, was conjugated to UCNP@PEG-maleimide. Disulfides 181-190 albumin Homo sapiens 11-24 33879435-0 2020 Thiol-disulfide exchange reactions occurring at modified bovine serum albumin detected using ellman"s reagent (5, 5"-dithiobis (2-itrobenzoic acid). Disulfides 6-15 albumin Homo sapiens 64-77 32369051-8 2020 The disulfide LMWG loaded with a thiol-containing protein (bovine serum albumin) features sustained release in vitro, whereas a dextran of the same molecular weight, lacking a thiol biomolecule, shows quick release. Disulfides 4-13 albumin Homo sapiens 66-79 31814373-7 2020 Conclusion: The results showed that thiol/disulfide homeostasis in patients with autoimmune gastritis caused an increase in ischemia modified albumin and disulfide whereas a decrease in thiols. Disulfides 42-51 albumin Homo sapiens 142-149 30028086-1 2018 Human serum albumin (HSA) is characterized by 17 disulfides and by only one unpaired cysteine (Cys34 ), which can be free in the reduced albumin or linked as a mixed disulfide with cysteine, or in minor amount with other natural thiols, in the oxidized albumin. Disulfides 49-59 albumin Homo sapiens 6-19 33417782-5 2019 In this study, bovine serum albumin (BSA) was self-assembled into sub-100 nm nanoparticles via an intermolecular disulfide network as the inner core. Disulfides 113-122 albumin Homo sapiens 22-35 30947639-4 2019 In this article, BSA was treated with urea and glutathione to prepare bovine serum albumin hydrogel controlled by two dynamic equilibrium bonds (disulfide and hydrogen bonds). Disulfides 145-154 albumin Homo sapiens 77-90 30514088-5 2018 Herein, a new self-assembly method based on a robust dye SQSS of which two squaraine molecules were conjugated through disulfide bond was developed for highly selective and sensitive detection of serum albumin (SA) in aqueous solution and live cells. Disulfides 119-128 albumin Homo sapiens 196-209 30351115-2 2018 Using serum albumin as a model, this study aims to expand our understanding of this relationship for a larger (66 kDa), multidomain protein that contains 17 internal disulfide bonds. Disulfides 166-175 albumin Homo sapiens 6-19 30028086-1 2018 Human serum albumin (HSA) is characterized by 17 disulfides and by only one unpaired cysteine (Cys34 ), which can be free in the reduced albumin or linked as a mixed disulfide with cysteine, or in minor amount with other natural thiols, in the oxidized albumin. Disulfides 49-58 albumin Homo sapiens 6-19 30005164-2 2018 In this study, human serum albumin was hybridized with hemoglobin by intermolecular disulfide bonds to develop a hybrid protein oxygen nanocarrier with chlorine e6 encapsulated (C@HPOC) for oxygen self-sufficient photodynamic therapy (PDT). Disulfides 84-93 albumin Homo sapiens 21-34 27685835-0 2016 The extreme hyper-reactivity of selected cysteines drives hierarchical disulfide bond formation in serum albumin. Disulfides 71-80 albumin Homo sapiens 99-112 28413192-1 2017 The secondary structural changes of human serum albumin with the intact 17 disulfide bridges (HSA) and the disulfide bridges-cleaved human serum albumin (RCM-HSA) in thermal denaturation were examined. Disulfides 75-84 albumin Homo sapiens 42-55 28413192-1 2017 The secondary structural changes of human serum albumin with the intact 17 disulfide bridges (HSA) and the disulfide bridges-cleaved human serum albumin (RCM-HSA) in thermal denaturation were examined. Disulfides 107-116 albumin Homo sapiens 139-152 28150932-5 2017 Here, PTX was incorporated in nontoxic and endogenous material, human serum albumin (HSA), via an innovative disulfide reduction method to construct HSA-based PTX nanoparticle (HSA-PTX NP) to not only realize redox-responsive drug release but also improve in vivo stability. Disulfides 109-118 albumin Homo sapiens 70-83 27062681-4 2016 From high-performance liquid chromatography spectra, we observed that one uremic solute binds to HD-ALB via the formation of disulfide bonds between HD-ALB and the uremic solute. Disulfides 125-134 albumin Homo sapiens 100-103 27685835-1 2016 After mild reduction of serum albumin, seven among the 34 cysteines forming the disulfide network displayed a surprising hyper-reactivity. Disulfides 80-89 albumin Homo sapiens 24-37 32263341-0 2016 Disulfide-crosslinked albumin hydrogels. Disulfides 0-9 albumin Homo sapiens 22-29 27251465-1 2016 Cooperative cascade catalysis by bovine serum albumin (BSA)-iodine allows for the first time the performance of C(sp(2))-H sulfenylation of indole from readily available thiophenol (-SH bond) via in situ generation/cleavage of disulfide (S-S bond) in air under aqueous conditions, whereas BSA or I2 individually do not permit this two step sequence to occur in the same pot towards C-S bond formation. Disulfides 227-236 albumin Homo sapiens 40-53 27766215-1 2016 Human serum albumin (HSA) is a non-glycosylated, negatively charged protein (Mw: about 65-kDa) that has one free cystein residue (Cys 34), and 17 disulfide bridges that these bridges have main role in its stability and longer biological life-time (15 to 19 days). Disulfides 146-155 albumin Homo sapiens 6-19 32263341-2 2016 In this study, we obtained disulfide-crosslinked albumin hydrogels using the protein"s own thiol groups. Disulfides 27-36 albumin Homo sapiens 49-56 32263341-3 2016 In the water solutions with denaturants such as urea and guanidinium, the disulfide-crosslinked albumin hydrogels showed a normal swelling profile. Disulfides 74-83 albumin Homo sapiens 96-103 26597547-2 2016 Pyridyl disulfide functionalized silica particles are prepared by surface chemical reactions, and thiol-terminated poly(oligo(ethylene glycol) monomethyl ether methacrylate) (POEGMA) and bovine serum albumin (BSA) molecules are grafted to the silica particles by thiol-disulfide exchange reactions. Disulfides 8-17 albumin Homo sapiens 194-207 22484442-0 2012 Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin. Disulfides 65-74 albumin Homo sapiens 91-104 26193081-0 2015 Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation. Disulfides 29-38 albumin Homo sapiens 55-68 25821118-1 2015 The inherently present seventeen disulfide bonds of the circulatory protein, human serum albumin (HSA) provide the necessary structural stability. Disulfides 33-42 albumin Homo sapiens 83-96 25821118-1 2015 The inherently present seventeen disulfide bonds of the circulatory protein, human serum albumin (HSA) provide the necessary structural stability. Disulfides 33-42 albumin Homo sapiens 98-101 25689578-0 2015 Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin. Disulfides 0-9 albumin Homo sapiens 79-92 25689578-3 2015 In this study, we report the effect of disulfide-reducing agent dithiothreitol (DTT) on hen egg white lysozyme (lysozyme) and bovine serum albumin (BSA) aggregation at pH 7.2 and 37 C. BSA and lysozyme proteins treated with disulfide-reducing agents form very distinct amorphous aggregates as observed by scanning electron microscope. Disulfides 39-48 albumin Homo sapiens 133-146 24569069-6 2014 Additionally, the binding of PAC induced the conformational changes of disulfide bridges of HSA with the decrease of alpha-helix content. Disulfides 71-80 albumin Homo sapiens 92-95 24256422-4 2013 By exposing disulfide-stabilized poly(methacrylic acid) nanoporous polymer particles (PMASH NPPs) to complete cell growth media containing 10% fetal bovine serum, a protein corona, with the most abundant component being bovine serum albumin, was characterized. Disulfides 12-21 albumin Homo sapiens 227-240 22899364-1 2012 The role of the 17 disulfide (S-S) bridges in preserving the native conformation of human serum albumin (HSA) is investigated by performing classical molecular dynamics (MD) simulations on protein structures with intact and, respectively, reduced S-S bridges. Disulfides 19-28 albumin Homo sapiens 90-103 23396533-0 2013 Human serum albumin (HSA) nanoparticles stabilized with intermolecular disulfide bonds. Disulfides 71-80 albumin Homo sapiens 6-19 22913736-3 2012 Time-resolved dynamic light scattering (DLS), disk centrifuge photosedimentometry (DCP), and circular dichroism (CD) spectroscopy studies confirm that bovine serum albumin (BSA) adsorbs rapidly onto the cationic poly(vinyl amine)-stabilized polypyrrole nanoparticles and suggest that the initial well-defined protein coronal is subsequently cross-linked via thiol-disulfide exchange. Disulfides 364-373 albumin Homo sapiens 158-171 18546891-3 2008 Using LC-ESITOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA. Disulfides 129-138 albumin Homo sapiens 96-99 21071845-1 2010 Since human serum albumin has one sulfhydryl group and 17 disulfides, reactive sulfhydryl groups give rise to heterogeneity. Disulfides 58-68 albumin Homo sapiens 12-25 21673386-7 2011 Therefore, human serum albumin can be fabricated into nanoparticles by breaking the disulfide bonds and these nanoparticles exhibit high tumor targeting ability. Disulfides 84-93 albumin Homo sapiens 17-30 21077590-5 2010 The 17 disulfide bridges present in HSA provide the necessary structural rigidity to the protein. Disulfides 7-16 albumin Homo sapiens 36-39 20609911-2 2010 The redox state of cysteine-34 of human albumin defines three fractions which allow to monitor albumin oxidation: mercaptalbumin with a free thiol group, nonmercaptalbumin1 containing a disulfide, and nonmercaptalbumin2 with a sulfinic or sulfonic acid group. Disulfides 186-195 albumin Homo sapiens 40-47 19462475-1 2009 Interferon-alpha2b (IFN-alpha2b) and human serum albumin (HSA) fusion protein (IFN-alpha2b-HSA) is a promising long acting formulation of IFN-alpha2b for the treatment of hepatitis C. However, accelerated mechanical and thermal stress tests revealed that IFN-alpha2b-HSA was prone to disulfide-linked aggregation. Disulfides 284-293 albumin Homo sapiens 43-56 18712897-2 2008 This study demonstrated that copper induced the disulfide-linkage between Tus, such as alpha-naphthylthiourea (ANTU) and fluorescein-5-isothiocyanate cadaverine (FTC), with albumin (Alb), a major carrier protein in plasma with multiple functions. Disulfides 48-57 albumin Homo sapiens 173-180 18712897-2 2008 This study demonstrated that copper induced the disulfide-linkage between Tus, such as alpha-naphthylthiourea (ANTU) and fluorescein-5-isothiocyanate cadaverine (FTC), with albumin (Alb), a major carrier protein in plasma with multiple functions. Disulfides 48-57 albumin Homo sapiens 182-185 18546891-3 2008 Using LC-ESITOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA. Disulfides 129-138 albumin Homo sapiens 188-191 17607746-5 2007 In turn, Alb-SS-X were dethiolated by the excess nonprotein SH groups because of the lower pK(a) value in mixed disulfide with respect to that of other thiols. Disulfides 112-121 albumin Homo sapiens 9-12 15499198-0 2004 Kinetic studies of covalent binding between N-acetyl-L-cysteine and human serum albumin through a mixed-disulfide using an N-methylpyridinium polymer-based column. Disulfides 104-113 albumin Homo sapiens 74-87 16857017-5 2006 Using LC-ESI-TOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA. Disulfides 130-139 albumin Homo sapiens 97-100 16857017-5 2006 Using LC-ESI-TOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA. Disulfides 130-139 albumin Homo sapiens 189-192 16343416-0 2006 Disulfide between Cys392 and Cys438 of human serum albumin is redox-active, which is responsible for the thioredoxin-supported lipid peroxidase activity. Disulfides 0-9 albumin Homo sapiens 45-58 15499198-1 2004 The binding properties of the disulfide covalent bond between N-acetyl-L-cysteine (NAC) and human serum albumin (HSA) were investigated. Disulfides 30-39 albumin Homo sapiens 98-111 15499198-1 2004 The binding properties of the disulfide covalent bond between N-acetyl-L-cysteine (NAC) and human serum albumin (HSA) were investigated. Disulfides 30-39 albumin Homo sapiens 113-116 11168369-0 2001 A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges. Disulfides 142-151 albumin Homo sapiens 108-121 12139771-1 2002 A high-performance liquid chromatographic (HPLC) analysis of human serum albumin (HSA) using an ion-exchange (DEAE-form) column shows three components: The principal component corresponds to human mercaptalbumin (HMA); the secondary to nonmercaptalbumin (HNA), having mixed disulfide with cystine (HNA[Cys]), or oxidized glutathione (HNA[Glut]); and the tertiary to HNA, oxidized more highly than mixed disulfide. Disulfides 274-283 albumin Homo sapiens 67-80 12139771-1 2002 A high-performance liquid chromatographic (HPLC) analysis of human serum albumin (HSA) using an ion-exchange (DEAE-form) column shows three components: The principal component corresponds to human mercaptalbumin (HMA); the secondary to nonmercaptalbumin (HNA), having mixed disulfide with cystine (HNA[Cys]), or oxidized glutathione (HNA[Glut]); and the tertiary to HNA, oxidized more highly than mixed disulfide. Disulfides 403-412 albumin Homo sapiens 67-80 12815038-9 2003 We validate the prediction that this site is chymase-susceptible by showing that chymase hydrolyzes albumin uniquely at the predicted location, with the resulting fragments remaining disulfide-linked. Disulfides 183-192 albumin Homo sapiens 100-107 11321671-0 2001 The electrochemically induced conformational transition of disulfides in bovine serum albumin studied by thin layer circular dichroism spectroelectrochemistry. Disulfides 59-69 albumin Homo sapiens 80-93 11321671-1 2001 The conformational transition of disulfides in bovine serum albumin (BSA) induced by electrochemical redox reaction of disulfides were monitored by in-situ circular dichroism (CD) spectroelectrochemistry, with a long optical path thin layer cell and analyzed by a singular value decomposition least square (SVDLS) method. Disulfides 33-43 albumin Homo sapiens 54-67 11321671-1 2001 The conformational transition of disulfides in bovine serum albumin (BSA) induced by electrochemical redox reaction of disulfides were monitored by in-situ circular dichroism (CD) spectroelectrochemistry, with a long optical path thin layer cell and analyzed by a singular value decomposition least square (SVDLS) method. Disulfides 119-129 albumin Homo sapiens 54-67 11777392-1 2001 Albumin polymers, having an average diameter of 1020 +/- 250 nm, were prepared by the disulfide polymerization of recombinant human serum albumin (rHSA) by controlling of the pH and temperature. Disulfides 86-95 albumin Homo sapiens 132-145 7882997-0 1995 A genetic variant of albumin (albumin Asola; Tyr140-->Cys) with no free -SH group but with an additional disulfide bridge. Disulfides 105-114 albumin Homo sapiens 21-28 9271208-4 1997 On the other hand, Raman spectra reveal pronounced CPT-induced local structural modifications of the HSA molecule, involving changes in configuration of the two disulfide bonds and transfer of a single Trp-residue to hydrophilic environment. Disulfides 161-170 albumin Homo sapiens 101-104 1634518-0 1992 Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation. Disulfides 30-39 albumin Homo sapiens 62-75 7509788-5 1994 The alpha ALB mRNA sequence encodes a predicted secreted protein with the typical triple domain disulfide cross-linked structure. Disulfides 96-105 albumin Homo sapiens 10-13 7806542-6 1994 Immunoblotting with antibodies directed against serum albumin demonstrated the presence of albumin covalently linked to fibrinogen via a disulfide bridge. Disulfides 137-146 albumin Homo sapiens 54-61 7806542-6 1994 Immunoblotting with antibodies directed against serum albumin demonstrated the presence of albumin covalently linked to fibrinogen via a disulfide bridge. Disulfides 137-146 albumin Homo sapiens 91-98 7969090-3 1994 However, here we show that rapid (10-min) uptake inhibitions by AA or by ROS generated by the xanthine plus xanthine oxidase (XO) reaction are selectively abolished by distinct agents; bovine serum albumin (BSA) acts only on AA, whereas the scavenger enzymes superoxide dismutase (SOD) and catalase (CAT) and the disulfide-reducing agent dithiothreitol (DTT) act only on ROS. Disulfides 313-322 albumin Homo sapiens 192-205 8373743-0 1993 Reactivity of 42 disulfides with thiol group of human haemoglobin and human serum albumin. Disulfides 17-27 albumin Homo sapiens 76-89 8373743-1 1993 The reactivities of disulfides of different compound families towards thiol groups of human haemoglobin and human serum albumin were determined at physiological pH 7.4 by anion-exchange liquid chromatography. Disulfides 20-30 albumin Homo sapiens 114-127 1285848-1 1992 The unfolded states of serum albumin, lysozyme and ribonuclease denatured in GuHCl with their disulfide bridges intact or reduced and carboxyamidomethylated have been compared by their circular dichroism, second-derivative and difference spectra in the ultraviolet region. Disulfides 94-103 albumin Homo sapiens 23-36 1634518-1 1992 The conformation of the fully disulfide-reduced state of human serum albumin was investigated by tryptophan fluorescence spectrum, CD analyses, and size-exclusion chromatography. Disulfides 30-39 albumin Homo sapiens 63-76 1634518-4 1992 The conformation of disulfide-reduced serum albumin was highly variable depending on pH and ionic strength conditions. Disulfides 20-29 albumin Homo sapiens 38-51 1634518-5 1992 Thus, we concluded that the disulfide-reduced state with partially folded variable conformation is involved in the reversible interconversion between the denatured reduced form and the native disulfide-bonded form of human serum albumin. Disulfides 28-37 albumin Homo sapiens 223-236 1634518-5 1992 Thus, we concluded that the disulfide-reduced state with partially folded variable conformation is involved in the reversible interconversion between the denatured reduced form and the native disulfide-bonded form of human serum albumin. Disulfides 192-201 albumin Homo sapiens 223-236 1897997-1 1991 We have reported recently that the disulfide groups in bovine serum albumin can be reduced by a radiolytic chain reaction which occurs in deoxygenated solutions containing formate ions. Disulfides 35-44 albumin Homo sapiens 62-75 2163967-8 1990 The preS2-bound part of the human serum albumin could be removed from HBsAg by high-salt, such as CsCl centrifugation, but another part could only be removed by treatment with a disulfide cleaving reagent. Disulfides 178-187 albumin Homo sapiens 34-47 1777934-1 1991 Long-term exposure to natural sun-light (UVA, UVB) induced fluorescence and caused disulfide bond formation in bovine serum albumin (BSA). Disulfides 83-92 albumin Homo sapiens 118-131 34386337-8 2021 Moreover, disulfide bond-containing prodrug/albumin nanoaggregates exhibit long circulation time and superior antitumor efficacy in vivo. Disulfides 10-19 albumin Homo sapiens 44-51 35189461-4 2022 This nanovaccine was constructed by linking bovine serum albumin (BSA) with the E7 antigen and then encapsulating the photosensitizer and adjuvant through disulfide bonds to form a highly biocompatible and stable structure. Disulfides 155-164 albumin Homo sapiens 51-64 35054674-6 2022 Once implemented, the thiol-disulfide exchange allowed the hydrogel dots to successfully capture and release the protein bovine serum albumin (BSA). Disulfides 28-37 albumin Homo sapiens 128-141