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ON THE INDIVIDUAL CHARACTERISTICS OF ANIMAL AMYLASES IN RELATION TO ENZYME SOURCE.

W R Thompson¹, I Friedman

¹Departments of Pathology and Surgery, Yale University School of Medicine, New Haven.

The Journal of General Physiology

|October 30, 2009

Summary

Amylase enzyme activity varies by species, not organ source. Hog and human amylases share a common active component, indicated by similar pH and UV light responses.

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Area of Science:

Biochemistry
Enzymology

Background:

Amylolytic enzymes are crucial for carbohydrate digestion.
Understanding amylase characteristics across different sources is important for biochemical research.

Purpose of the Study:

To investigate the individual characteristics of amylolytic enzymes from various animal sources.
To determine if amylase specificity is linked to the organ source or species.

Main Methods:

Enzymes from hog pancreatin, dog serum, human saliva, dog pancreatic extract, human pancreatic extract, and human serum were analyzed.
Viscosimetric methods were used to measure amylolytic activity.
Spontaneous inactivation and variations in relative activity with pH changes were compared.

Main Results:

Amylolytic activity in hog pancreatin and dog serum is attributed to single chemical entities.
Human saliva's amylolytic activity is primarily from a single, dissociable individual.
Dog pancreatic extract and human pancreatic extract/serum contain amylases identical to those found in dog serum and human saliva, respectively.
Hog and human amylases exhibit similar variations in activity with pH and sensitivity to UV light.

Conclusions:

Amylase specificity is determined by the species source, not the organ source.
Hog and human amylases likely share a common amylolytic radical.