INOSINE MONOPHOSPHATE DEHYDROGENASE FROM PORCINE (SUS-SCROFA-DOMESTICA) THYMUS - PURIFICATION AND PROPERTIES

Authors
PUGH ME SKIBO EB
Citation
Me. Pugh et Eb. Skibo, INOSINE MONOPHOSPHATE DEHYDROGENASE FROM PORCINE (SUS-SCROFA-DOMESTICA) THYMUS - PURIFICATION AND PROPERTIES, Comparative biochemistry and physiology. B. Comparative biochemistry, 105(2), 1993, pp. 381-387
Citations number
27
Categorie Soggetti
Biology
Journal title
Comparative biochemistry and physiology. B. Comparative biochemistry → ACNP
ISSN journal
03050491
Volume
105
Issue
2
Year of publication
1993
Pages
381 - 387
Database
ISI
SICI code
0305-0491(1993)105:2<381:IMDFP(>2.0.ZU;2-F
Abstract
1. IMP dehydrogenase (EC 1.1.1.205) from porcine thymus glands has bee n purified to homogeneity. 2. The enzyme has a subunit MW of 57 kDa an d an amino acid composition similar to those obtained from other norma l and cancerous mammalian cells. 3. The apparent K(m) values at pH 8.0 for IMP and NAD+ are 7 and 16 muM, respectively. 4. GMP, XMP and AMP are competitive inhibitors towards IMP with K(i) values of 50, 85 and 282 muM, respectively. 5. The effectiveness of nucleotides to protect inactivation by CI-IMP is IMP > GMP > XMP > AMP.