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T K Eto

Publications and source records attributed to T K Eto.

2 recordsLinked to original sources

Antifreeze glycoproteins increase solution viscosity.

A new microsensor that can analyze microliter volume samples was used to measure the viscosity of aqueous solutions of antifreeze glycoproteins as a function of temperature and concentration. The results show that at physiological concentrations which naturally occur in the fish, the antifreeze proteins significantly increase aqueous solution viscosity. The probability for ice nucleation is inversely proportional to viscosity. Therefore, the increased viscosity could explain, in part, reports on the beneficial effects of antifreeze glycoproteins during cryopreservation by vitrification. Reducing the probability for ice nucleation could be also beneficial for the survival of cold-water fish in their natural habitat. Millimolar concentrations of antifreeze proteins increase aqueous solution viscosity to values comparable with those of conventional cryoprotectants in molar concentrations.

Animals↗

Viscosity sensing with lamb-wave microsensor: dimethylsulfoxide solution viscosity as a function of temperature.

Recently, a new microsensor employing low-velocity ultrasonic Lamb waves was developed and demonstrated to be capable of measuring the viscosity of solutions in small volumes. The microsensor, when attached to a temperature-controlled stage, can measure viscosity as a function of temperature. In this investigation, the ultrasonic Lamb-wave oscillator is employed to experimentally measure the viscosity of dimethylsulfoxide (Me2SO) solutions as a function of temperature. The microsensor and the experimental procedure are described and results for 1M, 3M, and 5M Me2SO aqueous solutions are presented. Dimethylsulfoxide is a compound commonly employed as a cryoprotectant in cryopreservation, the low-temperature preservation of biological materials. The temperature dependence of viscosity obtained through this study can be used in determining the probability for ice nucleation in biological materials, a parameter of importance during cryopreservation.

Calibration↗