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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yoneda, Juliana Sakamoto Scanavachi, Gustavo Sebinelli, Heitor Gobbi Borges, Júlio Cesar Barbosa, Leandro R. S. Ciancaglini, Pietro Itri, Rosangela |
| Description | Country affiliation: Brazil Author Affiliation: Yoneda JS ( Instituto de Física da Universidade de São Paulo, IF USP, 05508-090 São Paulo, Brazil); Scanavachi G ( Instituto de Física da Universidade de São Paulo, IF USP, 05508-090 São Paulo, Brazil.); Sebinelli HG ( Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, FFCLRP USP, 14040-901 Ribeirão Preto, SP, Brazil.); Borges JC ( Instituto de Química de São Carlos, IQSC-USP, 13560-970 São Carlos, SP, Brazil.); Barbosa LR ( Instituto de Física da Universidade de São Paulo, IF USP, 05508-090 São Paulo, Brazil.); Ciancaglini P ( Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, FFCLRP USP, 14040-901 Ribeirão Preto, SP, Brazil.); Itri R ( Instituto de Física da Universidade de São Paulo, IF USP, 05508-090 São Paulo, Brazil. Electronic address: itri@if.usp.br.) |
| Abstract | In this work, we find an equilibrium between different Na,K-ATPase (NKA) oligomeric species solubilized in a non-ionic detergent C12E8 by means of Dynamic Light Scattering (DLS), Analytical Ultracentrifugation (AUC), Small Angle X-ray Scattering (SAXS), Spectrophotometry (absorption at 280/350nm) and enzymatic activity assay. The NKA sample after chromatography purification presented seven different populations as identified by AUC, with monomers and tetramers amounting to â¼55% of the total protein mass in solution. These two species constituted less than 40% of the total protein mass after increasing the NKA concentration. Removal of higher-order oligomer/aggregate species from the NKA solution using 220nm-pore filter resulted in an increase of the specific enzymatic activity. Nevertheless, the enzyme forms new large aggregates over an elapsed time of 20h. The results thus point out that C12E8-solubilized NKA is in a dynamic equilibrium of monomers, tetramers and high-order oligomers/subunit aggregates. These latter have low or null activity. High amount of detergent leads to the dissociation of NKA into smaller aggregates with no enzymatic activity. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Journal | International Journal of Biological Macromolecules |
| Volume Number | 89 |
| e-ISSN | 18790003 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-08-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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