title: Amino acid sequencing, molecular cloning and modelling of the chick liver class-theta glutathione S-transferase CL1.
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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002645:Chickens / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D005982:Glutathione Transferase / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000378:metabolism
chemical_list: D005982:Glutathione Transferase; C025097:Escherichia coli periplasmic proteinase; D012697:Serine Endopeptidases