Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10

Biochim Biophys Acta. 1994 Sep 13;1219(1):189-90. doi: 10.1016/0167-4781(94)90268-2.

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).

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Chaperonin 10
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • HeLa Cells
  • Heat-Shock Proteins / genetics*
  • Humans
  • Molecular Sequence Data
  • Regulatory Sequences, Nucleic Acid
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • Chaperonin 10
  • DNA, Complementary
  • Heat-Shock Proteins

Associated data

  • GENBANK/U07550