title: The primary structure of an Entamoeba histolytica beta-hexosaminidase A subunit.
abstract: An Entamoeba histolytica gene (hex-A1) that encodes subunit A of the lysosomal enzyme beta-hexosaminidase has been cloned and sequenced. The inferred 59 kDa hex-A1 protein has the same molecular weight and 32% amino acid residue identity with the human and mouse proteins and 28% residue identity with the Dictyostelium protein. Northern blot analysis identified a mRNA of approximately 1.6 kb, which is in agreement with the expected size of a mRNA encoding the 522 amino acid hex-A1 protein. Southern blot analysis indicated the presence of at least two beta-hexosaminidase A subunit genes.
authors.affiliation: Department of Microbiology and Immunology, Morehouse School of Medicine, Atlanta, Georgia 30310, USA.
authors.forename: M J
authors.initials: MJ
authors.lastname: Beanan
authors.forename: G B
authors.initials: GB
authors.lastname: Bailey
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D016054:DNA, Protozoan / Q000032:analysis; D004748:Entamoeba histolytica / Q000201:enzymology* / Q000235:genetics; D017125:Genes, Protozoan / Q000235:genetics; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D001619:beta-N-Acetylhexosaminidases / Q000737:chemistry* / Q000235:genetics
chemical_list: D016054:DNA, Protozoan; D001619:beta-N-Acetylhexosaminidases