title: Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase.
abstract: Three independent cDNAs coding for the erythrocyte isoform of human acylphosphatase were isolated and characterized. All the clones were incomplete at the 5' end, but Northern blot analysis using the cDNA as a probe showed the presence of an unusually long mRNA 5'-untranslated region. The transcript was present in a variety of human cell lines of different origins, although at different levels. Southern blot analysis on DNA from different individuals revealed a simple hybridization pattern. Large amounts of pure enzyme with kinetic characteristics very similar to those of the native protein were expressed in E. coli.
authors.affiliation: Department of Biochemical Sciences, University of Florence, Italy.
authors.forename: T
authors.initials: T
authors.lastname: Fiaschi
authors.forename: G
authors.initials: G
authors.lastname: Raugei
authors.forename: R
authors.initials: R
authors.lastname: Marzocchini
authors.forename: P
authors.initials: P
authors.lastname: Chiarugi
authors.forename: P
authors.initials: P
authors.lastname: Cirri
authors.forename: G
authors.initials: G
authors.lastname: Ramponi
mesh_terms: D017766:Acid Anhydride Hydrolases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D002460:Cell Line; D018076:DNA, Complementary / Q000235:genetics; D004912:Erythrocytes / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics; D017422:Sequence Analysis, DNA; D000097024:Acylphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D018076:DNA, Complementary; D007527:Isoenzymes; D012333:RNA, Messenger; D000097024:Acylphosphatase