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LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
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Chemistry
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JoVE Journal Chemistry
LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations

DOI:
10.3791/4189-v

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09:32 min

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February 04, 2013

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,
1Institute of Biochemistry, Food Science, and Nutrition , The Robert H. Smith Faculty of Agriculture, Food, and Environment,The Hebrew University of Jerusalem, 2Department of Physics and Astronomy,Ohio University

Chapters

  • 00:05Title
  • 01:28Preliminary Procedures
  • 03:10Sample Preparation
  • 04:32Thermal Hysteresis (TH) Activity Measurement
  • 07:13Measurement of the Time-dependent TH Activity
  • 08:05Results: MpIBP TH Activity as a Function of Ice Crystal Exposure Time to the IBPs
  • 09:01Conclusion

Summary

Automatic Translation

Automatic Translation

Ice binding proteins (IBPs), also known as antifreeze proteins, inhibit ice growth and are a promising additive for use in the cryopreservation of tissues. The main tool used to investigate IBPs is the nanoliter osmometer. We developed a home-designed cooling stage mounted on an optical microscope and controlled using a custom-built LabVIEW routine. The nanoliter osmometer described here manipulated the sample temperature in an ultra-sensitive manner.

Tags

LabVIEWNanoliter OsmometerIce-binding ProteinsAntifreeze ProteinsIce Structuring ProteinsThermal Hysteresis ProteinsIce Recrystallization Inhibition ProteinsCold-adapted OrganismsFishPlantsArthropodsFungiBacteriaAdsorptionIce CrystalsGibbs-Thomson EffectDepressionThermal HysteresisNanoliter Osmometer MeasurementsClifton InstrumentOtago InstrumentOsmolarityMelting Point Depression

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