title: Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10.
abstract: A full-length cDNA clone encoding chaperonin 10 (cpn10) from a HeLa cell cDNA library was isolated. The cDNA is 538 bp in length, contains an ATG codon and a putative polyadenylation signal, and specifies a protein of 102 amino acids. Immunoprecipitation experiment showed that this human cpn10 has an apparent molecular mass of 11 kDa in sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
authors.affiliation: Department of Dermatology, New England Medical Center, Boston, MA 02111.
authors.forename: J J
authors.initials: JJ
authors.lastname: Chen
authors.forename: D J
authors.initials: DJ
authors.lastname: McNealy
authors.forename: S
authors.initials: S
authors.lastname: Dalal
authors.forename: E J
authors.initials: EJ
authors.lastname: Androphy
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D018835:Chaperonin 10; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D012045:Regulatory Sequences, Nucleic Acid; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
chemical_list: D018835:Chaperonin 10; D018076:DNA, Complementary; D006360:Heat-Shock Proteins