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Expression, Purification, and Biochemical Characterization of Human Afamin
Journal of Proteome Research, 17 (2018), 3; 1269-1277. https://doi.org/10.1021/acs.jproteome.7b00867
Altamirano, Alessandra; Naschberger, Andreas; Fürnrohr, Barbara G.; Saldova, Radka; Struwe, Weston B.; Jennings, Patrick M.; Millán Martín, Silvia; Malić, Suzana; Plangger, Immanuel; Lechner, Stefan; Pisano, Reina; Peretti, Nicole; Linke, Bernd; Aguiar, Mario M.; Fresser, Friedrich; Ritsch, Andreas; Lenac Roviš, Tihana; Goode, Christina; Rudd, Pauline M.; Scheffzek, Klaus; Rupp, Bernhard; Dieplinger, Hans Više autora...

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Altamirano, A., Naschberger, A., Fürnrohr, B. G., Saldova, R., Struwe, W. B., Jennings, P. M. ... Dieplinger, H. (2018). Expression, Purification, and Biochemical Characterization of Human Afamin. Journal of Proteome Research, 17. (3), 1269-1277. doi: 10.1021/acs.jproteome.7b00867

Altamirano, Alessandra, et al. "Expression, Purification, and Biochemical Characterization of Human Afamin." Journal of Proteome Research, vol. 17, br. 3, 2018, str. 1269-1277. https://doi.org/10.1021/acs.jproteome.7b00867

Altamirano, Alessandra, Andreas Naschberger, Barbara G. Fürnrohr, Radka Saldova, Weston B. Struwe, Patrick M. Jennings, Silvia Millán Martín, et al. "Expression, Purification, and Biochemical Characterization of Human Afamin." Journal of Proteome Research 17, br. 3 (2018): 1269-1277. https://doi.org/10.1021/acs.jproteome.7b00867

Altamirano, A., et al. (2018) 'Expression, Purification, and Biochemical Characterization of Human Afamin', Journal of Proteome Research, 17(3), str. 1269-1277. doi: 10.1021/acs.jproteome.7b00867

Altamirano A, Naschberger A, Fürnrohr BG, Saldova R, Struwe WB, Jennings PM, i sur.. Expression, Purification, and Biochemical Characterization of Human Afamin. Journal of Proteome Research [Internet]. 2018. [pristupljeno 19.12.2024.];17(3):1269-1277. doi: 10.1021/acs.jproteome.7b00867

A. Altamirano, et al., "Expression, Purification, and Biochemical Characterization of Human Afamin", Journal of Proteome Research, vol. 17, br. 3, str. 1269-1277, 2018. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:184:777985. [Citirano: 19.12.2024.]

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Naslov (engleski)Expression, Purification, and Biochemical Characterization of Human Afamin
AutorAlessandra Altamirano
AutorAndreas Naschberger
AutorBarbara G. Fürnrohr
AutorRadka Saldova
AutorWeston B. Struwe
AutorPatrick M. Jennings
AutorSilvia Millán Martín
AutorSuzana Malić
AutorImmanuel Plangger
AutorStefan Lechner
AutorReina Pisano
AutorNicole Peretti
AutorBernd Linke
AutorMario M. Aguiar
AutorFriedrich Fresser
AutorAndreas Ritsch
AutorTihana Lenac Roviš
AutorChristina Goode
AutorPauline M. Rudd
AutorKlaus Scheffzek
AutorBernhard Rupp
AutorHans Dieplinger
Autorova ustanovaSveučilište u Rijeci
Medicinski fakultet
(Centar za proteomiku)
Znanstveno / umjetničko
područje, polje i grana		BIOMEDICINA I ZDRAVSTVO
Temeljne medicinske znanosti
Sažetak (engleski)
Afamin is an 87 kDa glycoprotein with five predicted N-glycosylation sites. Afamin's glycan abundance contributes to conformational and chemical inhomogeneity presenting great challenges for molecular structure determination. For the purpose of studying the structure of afamin, various forms of recombinantly expressed human afamin (rhAFM) with different glycosylation patterns were thus created. Wild-type rhAFM and various hypoglycosylated forms were expressed in CHO, CHO-Lec1, and HEK293T cells. Fully nonglycosylated rhAFM was obtained by transfection of point-mutated cDNA to delete all N-glycosylation sites of afamin. Wild-type and hypo/nonglycosylated rhAFM were purified from cell culture supernatants by immobilized metal ion affinity and size exclusion chromatography. Glycan analysis of purified proteins demonstrated differences in micro- and macro-heterogeneity of glycosylation enabling the comparison between hypoglycosylated, wild- type rhAFM, and native plasma afamin. Because antibody fragments can work as artificial chaperones by stabilizing the structure of proteins and consequently enhance the chance for successful crystallization, we incubated a Fab fragment of the monoclonal anti-afamin antibody N14 with human afamin and obtained a stoichiometric complex. Subsequent results showed sufficient expression of various partially or nonglycosylated forms of rhAFM in HEK293T and CHO cells and revealed that glycosylation is not necessary for expression and secretion
Ključne riječi (engleski)
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran - međunarodna recenzija
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaJournal of Proteome Research
Brojčani podacivol. 17, br. 3, str. 1269-1277
p-ISSN1535-3893
DOIhttps://doi.org/10.1021/acs.jproteome.7b00867
URN:NBNurn:nbn:hr:184:777985
Datum objave publikacije2018
URL dokumentahttp://bib.irb.hr/1049761
Vrsta resursaTekst
Prava pristupaZatvoreni pristup
Uvjeti korištenjaIkona licence Zaštićeno autorskim pravom.
Datum i vrijeme pohrane2022-02-21 11:58:42