Characterization of adenosine deaminase from normal human epidermis and squamous cell carcinoma of the skin.

We compared the characteristics of adenosine deaminases (ADs) (E.C. 3.5.4.4.) in squamous cell carcinoma and normal human epidermis. Increased specific activity (per mg protein) of AD was observed in squamous cell carcinoma compared with that of the normal epidermis. In normal human epidermis most of the AD existed as a large form (Mr 300,000-350,000, type A). Squamous cell carcinoma of the skin was characterized by a high proportion of small-form (Mr 30,000-40,000, type C) AD. The proportion of the small-form enzyme varied from tumor to tumor. Comparison of the large-form AD from squamous cell carcinoma to that from normal epidermis revealed that both enzymes were similar in relative substrate specificity, Km values for adenosine, pH optima, heat stability pattern, isoelectric point, and sensitivity to inhibition by coformycin, a tight binding inhibitor of AD. However, the low molecular weight of AD from squamous cell carcinoma was less heat stable than that from the large-molecular-weight form. Increased AD activity and the high proportion of the small form of AD might be significant features of squamous cell carcinoma of the skin.