Structural studies on the freezing-point-depressing protein of the winter flounder Pseudopleuronectes americanus

摘要: Abstract The freezing-point-depressing protein from the winter flounder, Pseudopleuronectes americanus has been shown circular dichroism measurements to possess a large proportion (∼85%) of α-helical conformation in aqueous solution (pH 8.0) at −1°C. helical content decreases as temperature is raised. Viscosity data −1°C indicate an asymmetric shape for molecule compatible with its high content. Thus, secondary and tertiary structure this well primary (reported elsewhere), are found be different counterpart glycoproteins isolated Antarctic fish.