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The Primary Structure of an Entamoeba histolytica β‐Hexosaminidase A Subunit
Author(s) -
BEANAN MAUREEN J.,
BAILEY GORDON B.
Publication year - 1995
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1995.tb05919.x
Subject(s) - entamoeba histolytica , biology , protein subunit , hexosaminidase , microbiology and biotechnology , gene , western blot , northern blot , amino acid , messenger rna , biochemistry , peptide sequence , residue (chemistry) , protein primary structure , enzyme , genetics
ABSTRACT. An Entamoeba histolytica gene ( hex‐A1 ) that encodes subunit A of the lysosomal enzyme β‐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 β‐hexosaminidase A subunit genes.