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In Situ Monitoring of Diffusion of Guest Molecules in Porous Media Using Electron Paramagnetic Resonance Imaging

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THE DIFFUSION COEFFICIENT OF CRYSTALLINE TRYPSIN.

¹Laboratories of The Rockefeller Institute for Medical Research.

The Journal of General Physiology

|October 30, 2009

Summary

The diffusion coefficient for crystalline trypsin was measured at 5°C. Proteolytic activity and protein nitrogen diffused at the same rate, suggesting a chemical bond.

Area of Science:

Biochemistry
Physical Chemistry

Background:

Understanding protein diffusion is crucial for biochemical processes.
Crystalline trypsin is a key enzyme in protein digestion.

Purpose of the Study:

To determine the diffusion coefficient of crystalline trypsin.
To investigate the relationship between proteolytic activity and protein diffusion.

Main Methods:

Diffusion experiments were conducted using crystalline trypsin in a 0.5 saturated magnesium sulfate solution.
Measurements were taken at a controlled temperature of 5°C.
The diffusion rates of proteolytic activity and protein nitrogen were compared.

Main Results:

The diffusion coefficient of crystalline trypsin was determined to be 0.020 +/-0.001 cm²/day.

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This corresponds to a molecular radius of 2.6 x 10⁻⁷ cm.

The diffusion rates of proteolytic activity and protein nitrogen were found to be identical.

Conclusions:

Proteolytic activity and protein nitrogen are chemically combined within crystalline trypsin.
The enzyme does not exist as a simple adsorption complex.