| Literature DB >> 7492340 |
C D Hsiao1, E O Martsen, J Y Lee, S P Tsai, M F Tam.
Abstract
Glutathione S-transferase CL1-2 heterodimers purified from 1-day-old chick livers were digested with Achromobacter proteinase I. The resulting fragments were separated for amino acid sequence analysis. Oligonucleotide probes were constructed based on sequence similarity to class-Theta glutathione S-transferases for PCR using a chicken liver cDNA library as template. A full-length clone (1725 bp) encoding a polypeptide comprising 261 amino acids was isolated. Including conservative substitutions, this protein has 70-73% sequence similarity with other mammalian class-Theta glutathione S-transferases. Based on known X-ray crystal structures of class-Alpha, -Mu and -Pi glutathione S-transferases, a model is constructed for the N-terminal 232 residues of CL1.Entities:
Mesh:
Substances:
Year: 1995 PMID: 7492340 PMCID: PMC1136231 DOI: 10.1042/bj3120091
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857