| Institution: | 1. Department of Microbiology, Oregon State University, Corvallis, OR 97331, U.S.A.;2. Surgical Research Laboratory, Veterans Administration Medical Center, Portland, OR 97201 U.S.A.;3. Department of Microbiology and Immunology and Department of Neurology, University of Oregon, Health Sciences Center, Portland, OR 97201, U.S.A. |
| Abstract: | 5'-Deoxy-5'-methylthioadenosine (MTA) phosphorylase was purified 13.4-fold from human peripheral lymphocytes. The enzyme demonstrated normal Michaelis-Menten kinetics with Km values of 26 microM and 7.5 mM for the two substrates, MTA and phosphate, respectively. The rate of MTA degradation was temperature dependent, 47 degrees being the optimum temperature. Five structural analogs served as alternative substrates with Km values ranging from 31 to 53 microM while two compounds, 5'-deoxy-5'-methylthiotubercidin (MTT) (Ki = 31 microM) and adenine (Ki = 172 microM), were inhibitory. These same analogs were examined as inhibitors of mitogen-induced human lymphocyte blastogenesis. MTT was found to be the most effective inhibitor of lymphocyte transformation with an I50 of 80 microM. |
