title: Oxidative folding of nerve growth factor can be mediated by the pro-peptide of neurotrophin-3.
abstract: We have previously shown that the pro-peptide of human nerve growth factor (NGF) facilitates oxidative folding of the mature part. For the analysis of functional specificities of the pro-peptides of NGF and the related neurotrophin-3 (NT-3) with respect to structure formation, chimeric proteins with swapped pro-peptides were generated. Neither the structure nor the stability of the mature domains was influenced by the heterologous pro-peptides. For the pro-peptide of NT-3 fused to the mature part of NGF, stabilization of the pro-peptide moiety by the NGF part was observed. Folding kinetics and renaturation yields of this chimeric protein were comparable to those of proNGF. Our results demonstrate functional interchangeability between the pro-peptides of NGF and NT-3 with respect to their role in assisting oxidative folding of the mature part.
authors: Institut für Biotechnologie der Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle, Germany.
authors: Anja
authors: A
authors: Hauburger
authors: Marco
authors: M
authors: Kliemannel
authors: Peder
authors: P
authors: Madsen
authors: Rainer
authors: R
authors: Rudolph
authors: Elisabeth
authors: E
authors: Schwarz
mesh_terms: D002942:Circular Dichroism; D005682:Gadolinium / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D020932:Nerve Growth Factor / Q000737:chemistry* / Q000378:metabolism*; D020933:Neurotrophin 3 / Q000378:metabolism*; D010084:Oxidation-Reduction / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013050:Spectrometry, Fluorescence
chemical_list: D020933:Neurotrophin 3; D011498:Protein Precursors; D011994:Recombinant Proteins; D020932:Nerve Growth Factor; D005682:Gadolinium; C038958:gadolinium chloride