| Literature DB >> 1959626 |
A M Tommey1, J Shi, W P Lindsay, P E Urwin, N J Robinson.
Abstract
The pea (Pisum sativum L.) gene PSMTA has an ORF encoding a predicted protein with sequence similarity to class I metallothioneins (MTS). To examine the metal-binding properties of the PSMTA protein it has been expressed in E. coli as a carboxyterminal extension of glutathione-S-transferase (GST). Metal ions were associated with the expressed protein when purified from lysates of E. coli grown in metal supplemented media. The pH of half-dissociation of Zn, Cd and Cu ions from the recombinant fusion protein was determined to be 5.35, 3.95 and 1.45 respectively, compared with equivalent estimates of 4.50, 3.00 and 1.80 for equine renal MT.Entities:
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Year: 1991 PMID: 1959626 DOI: 10.1016/0014-5793(91)80831-m
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124