The diversity of glycan chains in jellyfish mucin of three Cubozoan species: the contrast in molecular evolution rates of the peptide chain and Glycans.

The O-glycan composition of jellyfish (JF) mucin (qniumucin: Q-mucin) extracted from three Cubozoan species was studied after the optimization of the purification protocol. Application of a stepwise gradient of ionic strength to anion exchange chromatography (AEXC) was effective for isolating Q-mucin from coexisting impurities. In the three species, the amino acid sequence of the tandem repeat (TR) region in Q-mucin in all three Cubozoans seemed to remain the same as that in all Scyphozoans, although their glycan chains seemed to exhibit clear diversity.

Preparation of Jellyfish Mucin.

A mucin-type glycoprotein extracted from various species of jellyfish (JF) is named qniumucin (Q-mucin). Compared with general mucins, most of which are from mammals including humans, Q-mucin can be collected on a relatively large scale with high yield. Owing to its simple structure with low heterogeneity, Q-mucin has a potential to be developed into material mucins which opens various applications valuable to humans.

DNA-binding protein from starvation cells traps intracellular free-divalent iron and plays an important role in oxidative stress resistance in Acetobacter pasteurianus NBRC 3283.

Acetobacter pasteurianus accumulates reactive oxygen species (ROS). ROS are produced by electron and oxygen coupling in the electron transport chain in the intracellular environment during the stationary and in the acetic acid over-oxidation phases in the presence of ethanol, thereby exposing cell to oxidative stress. In this study, to reveal the resistance mechanism to oxidative stress in A.