Linear polymerization caused by the defective folding of a non-inhibitory serpin ovalbumin

Journal of Biochemistry
Nobuaki ShiraiK Yasumoto

Abstract

Polymerization caused by defective folding of heat-denatured ovalbumin was examined. A compactly misfolded ovalbumin that was produced by cooling heat-denatured protein rapidly tended to aggregate in the presence of salt. Two different forms of aggregates were observed as the concentration of salt was varied: a linear polymer at a physiological concentration and a massive agglomerate at a higher concentration. Salt-induced polymerization depended on the species of anion and the order of effectiveness followed the lyotropic series of Hofmeister. Defective folding of heat-denatured ovalbumin induced the exposure of cysteine residues in sequences located in the interior of the native protein. The misfolded ovalbumin, but not the native protein, bound to bovine BiP and stimulated its ATPase activity with the K(m) of 64 microM and the V(max) of 0.5 nmol/min per milligram. Measurement of surface plasmon resonance revealed that only the misfolded ovalbumin was recognized with the K(d) of 4.12 X 10(-8) M by the Fab fragment of a monoclonal antibody raised against hen ovalbumin, and its epitope was determined to be a hydrophobic segment in the beta-strand of central sheet A. Transmission electron microscopy showed that the linear polyme...Continue Reading

Citations

Feb 6, 2002·Bioscience, Biotechnology, and Biochemistry·Y Sun, S Hayakawa
Jul 2, 2003·Bioscience, Biotechnology, and Biochemistry·Fumito TaniNaofumi Kitabatake
Dec 4, 2014·APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica·Bettina Eide HolmNicole Hartwig Trier
Sep 27, 2016·Scientific Reports·Benjamin T PorebskiAshley M Buckle
Oct 29, 2002·Biotechnology and Bioengineering·Hung D Nguyen, Carol K Hall
Dec 25, 2004·Bioscience, Biotechnology, and Biochemistry·Fumito TaniNaofumi Kitabatake
Mar 1, 2006·Analytical Chemistry·Caroline TokarskiCécile Cren-Olivé
Aug 22, 2001·Journal of Agricultural and Food Chemistry·A HandaN Kuroda

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