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We began analyzing https://link.springer.com/article/10.1007/s11064-012-0923-x, but it redirected us to https://link.springer.com/article/10.1007/s11064-012-0923-x. The analysis below is for the second page.

Title[redir]:
HSPA5 Forms Specific Complexes with Copper | Neurochemical Research
Description:
Our previous study indicated that Hspa5 directly interacts with copper (Cu) to maintain Cu homeostasis in astrocytes. In this study, we explored the possibility that Cu forms a specific complex with Hspa5 by assaying stoichiometric binding of Cu and other metals to recombinant human HSPA5 (rh-HSPA5) in silico. Spectrophotometric analysis showed that incubation of rh-HSPA5 with Cu but not with Fe, Mn, Zn, or Pb in the presence of ascorbic acid produced an absorbance peak at 470 nm. Furthermore, the absorbance peak was absent when bovine serum albumin was incubated with Cu and when another recombinant protein YWHAZ-14-3-3-Zeta carrying a 6× histidine tag identical to the tag in the rh-HSPA5 was incubated with Cu. The absorbance peak produced by Cu and rh-HSPA5 was abolished by EDTA treatment and was stabilized at pH levels above 6.5. Assay of the stoichiometry of metal binding to the purified rh-HSPA5 showed that one molecule of the rh-HSPA5 could chelate 1 or 2 Cu, 13 iron (Fe), 5 zinc (Zn) and 10 lead (Pb) ions but not manganese (Mn). These data further support our previous finding that HSPA5 specifically forms a complex with Cu to help maintain Cu homeostasis.

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article, google, scholar, pubmed, cas, copper, qian, hspa, zheng, res, rhhspa, alzheimers, disease, brain, privacy, cookies, content, data, research, november, zhang, astrocytes, lead, access, chaperone, information, publish, search, forms, complexes, meng, complex, human, absorbance, serum, metal, grp, neurochem, log, journal, specific, yongchang, bingchao, xuchu, taylor, tiffanycastiglioni, homeostasis, binding, peak, albumin,

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month download article/chapter 78-kda glucose-regulated protein grp78/bip suppress misfolding amino-terminal peptide fragment copper-induced ros generation lead-induced oxidative stress purified rh-hspa5 showed full article pdf related subjects specific complex hspa5 specifically forms qian yc privacy choices/manage cookies recombinant human hspa5 article qian endoplasmic reticulum stress defective chaperone biology grp78 compartmentalized redistribution molecular chaperone hspa5 hspa5 directly interacts copper-induced damage spectrophotometric analysis showed low plasma concentrations lead targets grp78 chaperone proteins hsp70 european economic area batch adsorption systems spin hamiltonian parameters pajonk fg van dyke br alicia marroquin-cardona veterinary integrative biosciences lower plasma copper copper handling machinery assaying stoichiometric binding conditions privacy policy ascorbic acid produced cognitive decline correlates amyloid-beta peptides yongchang qian bovine serum albumin article log author information authors accepting optional cookies serum copper levels absorbance peak produced copper-binding properties high affinity site metal binding pb-treated glia

Schema {🗺️}

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         description:Our previous study indicated that Hspa5 directly interacts with copper (Cu) to maintain Cu homeostasis in astrocytes. In this study, we explored the possibility that Cu forms a specific complex with Hspa5 by assaying stoichiometric binding of Cu and other metals to recombinant human HSPA5 (rh-HSPA5) in silico. Spectrophotometric analysis showed that incubation of rh-HSPA5 with Cu but not with Fe, Mn, Zn, or Pb in the presence of ascorbic acid produced an absorbance peak at 470 nm. Furthermore, the absorbance peak was absent when bovine serum albumin was incubated with Cu and when another recombinant protein YWHAZ-14-3-3-Zeta carrying a 6× histidine tag identical to the tag in the rh-HSPA5 was incubated with Cu. The absorbance peak produced by Cu and rh-HSPA5 was abolished by EDTA treatment and was stabilized at pH levels above 6.5. Assay of the stoichiometry of metal binding to the purified rh-HSPA5 showed that one molecule of the rh-HSPA5 could chelate 1 or 2 Cu, 13 iron (Fe), 5 zinc (Zn) and 10 lead (Pb) ions but not manganese (Mn). These data further support our previous finding that HSPA5 specifically forms a complex with Cu to help maintain Cu homeostasis.
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      description:Our previous study indicated that Hspa5 directly interacts with copper (Cu) to maintain Cu homeostasis in astrocytes. In this study, we explored the possibility that Cu forms a specific complex with Hspa5 by assaying stoichiometric binding of Cu and other metals to recombinant human HSPA5 (rh-HSPA5) in silico. Spectrophotometric analysis showed that incubation of rh-HSPA5 with Cu but not with Fe, Mn, Zn, or Pb in the presence of ascorbic acid produced an absorbance peak at 470 nm. Furthermore, the absorbance peak was absent when bovine serum albumin was incubated with Cu and when another recombinant protein YWHAZ-14-3-3-Zeta carrying a 6× histidine tag identical to the tag in the rh-HSPA5 was incubated with Cu. The absorbance peak produced by Cu and rh-HSPA5 was abolished by EDTA treatment and was stabilized at pH levels above 6.5. Assay of the stoichiometry of metal binding to the purified rh-HSPA5 showed that one molecule of the rh-HSPA5 could chelate 1 or 2 Cu, 13 iron (Fe), 5 zinc (Zn) and 10 lead (Pb) ions but not manganese (Mn). These data further support our previous finding that HSPA5 specifically forms a complex with Cu to help maintain Cu homeostasis.
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