3.1.6.8 ? x * 62000, SDS-PAGE 708615 3.1.6.8 dimer 1 * 49000, 1 * 55000, SDS-PAGE 135681 3.1.6.8 dimer 2 * ca. 55000, SDS-PAGE 135686 3.1.6.8 dimer 2 x 77000, SDS-PAGE 668313 3.1.6.8 dimer at pH 6.5-6.7, the enzyme exists in solution as a dimer 649125 3.1.6.8 dimer at pH above 6, the enzyme exists in solution as a dimer 650583 3.1.6.8 dimer between pH 5.5-6.5, depends also on ionic strength 135554 3.1.6.8 dimer mature enzyme 714958 3.1.6.8 homodimer at neutral pH 649289 3.1.6.8 homooctamer at acidic pH 649289 3.1.6.8 monomer 1 * 140000, each monomer consists of 2 equivalent polypeptide chains 135684, 135695 3.1.6.8 monomer 1 * 66000, SDS-PAGE 681035 3.1.6.8 monomer at pH 5.6 monomer, at pH 4.8 tetramer 135554, 135679, 135695 3.1.6.8 additional information mature lysosomal arylsulfatase A forms dimers at neutral pH, while in the early biosynthetic pathway, arylsulfatase A forms oligomers with more than two subunits. Within a heteromer, the misfolded subunit exerts a dominant negative effect on the wild-type subunit 714958 3.1.6.8 additional information The dimer-octamer equilibrium is regulated by the pH and may be explained by a switch function of Glu424. Glu424 in the conformation suitable for the intramolecular hydrogen bonds to Gln460. Glu424 in the conformation suitable for the intermolecular hydrogen bonds to Phe398 650583 3.1.6.8 additional information the polypeptide complexes, rather than the monomers, are subject to endoplasmic reticulum quality control and, within a heteromer, the misfolded subunit exerts a dominant negative effect on the wild-type subunit 714779 3.1.6.8 octamer ar pH 5.0-5.4, the enzyme exists in solution as a dimer or as an octamer 649125 3.1.6.8 octamer at pH below 6, the enzyme exists in solution as octamer 650583 3.1.6.8 octamer tetramer of dimers 135692 3.1.6.8 oligomer early enzyme 714958 3.1.6.8 oligomer x * 63000, x * 59000, ratio 1.9:1, SDS-PAGE 135666 3.1.6.8 tetramer aggregation to tetramer at higher concentrations around pH 5, 2 * 49000, 2 * 55000 135681 3.1.6.8 tetramer at pH 4.8 tetramer, at pH 5.6 monomer 135679