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 μM and 7.5 mM for the two substrates. MTA and phosphate, respectively. The rate of MTA degradation was temperature dependent, 47° being the optimum temperature. Five structural analogs served as alternative substrates with Km values ranging from 31 to 53 μM while two compounds, 5'-deoxy-5'methylthiotubercidin (MTT) (Ki = 31 μM) and adenine (Ki = 172 μM), 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 μM.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 503-507 |
| Number of pages | 5 |
| Journal | Biochemical Pharmacology |
| Volume | 31 |
| Issue number | 4 |
| DOIs | |
| State | Published - Feb 15 1982 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Pharmacology
Cite this
Structural analogs of 5'-methylthioadenosine as substrates and inhibitors of 5'-methylthioadenosine phosphorylase and as inhibitors of human lymphocyte transformation. / White, Michael W.; Vandenbark, Arthur; Barney, Carolyn L.; Ferro, Adolph J.
In: Biochemical Pharmacology, Vol. 31, No. 4, 15.02.1982, p. 503-507.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural analogs of 5'-methylthioadenosine as substrates and inhibitors of 5'-methylthioadenosine phosphorylase and as inhibitors of human lymphocyte transformation
AU - White, Michael W.
AU - Vandenbark, Arthur
AU - Barney, Carolyn L.
AU - Ferro, Adolph J.
PY - 1982/2/15
Y1 - 1982/2/15
N2 - 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 μM and 7.5 mM for the two substrates. MTA and phosphate, respectively. The rate of MTA degradation was temperature dependent, 47° being the optimum temperature. Five structural analogs served as alternative substrates with Km values ranging from 31 to 53 μM while two compounds, 5'-deoxy-5'methylthiotubercidin (MTT) (Ki = 31 μM) and adenine (Ki = 172 μM), 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 μM.
AB - 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 μM and 7.5 mM for the two substrates. MTA and phosphate, respectively. The rate of MTA degradation was temperature dependent, 47° being the optimum temperature. Five structural analogs served as alternative substrates with Km values ranging from 31 to 53 μM while two compounds, 5'-deoxy-5'methylthiotubercidin (MTT) (Ki = 31 μM) and adenine (Ki = 172 μM), 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 μM.
UR - http://www.scopus.com/inward/record.url?scp=0020047761&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0020047761&partnerID=8YFLogxK
U2 - 10.1016/0006-2952(82)90151-4
DO - 10.1016/0006-2952(82)90151-4
M3 - Article
C2 - 6802139
AN - SCOPUS:0020047761
VL - 31
SP - 503
EP - 507
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
SN - 0006-2952
IS - 4
ER -