STUDIES ON CRYSTALLINE UREASE : IV. THE "ANTITRYPTIC" PROPERTY OF CRYSTALLINE UREASE

Area of Science:

• Biochemistry
• Enzymology

Background:

• Urease is a crucial enzyme involved in urea hydrolysis.
• Understanding enzyme-inhibitor interactions is vital for biochemical research.

Purpose of the Study:

• To investigate the interaction between crystalline urease and trypsin.
• To elucidate the role of gums in modulating this interaction.

Main Methods:

• Enzyme activity assays were performed on crystalline urease.
• Experiments involved varying the presence and order of addition of trypsin and gum.

Main Results:

• Trypsin alone acted as a protective colloid for urease, preventing its inactivation.
• In the presence of gum, trypsin rapidly inactivated urease.
• Pre-incubation of urease with trypsin before gum addition prevented inactivation.

Conclusions:

• The findings suggest urease possesses an 'antitrypsin' group, forming an inactive complex with trypsin.
• Gum interferes with this complex formation by binding to urease, allowing trypsin to digest it.
• This interaction supports the protein nature of urease.