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Cloning and sequence analysis of a cDNA encoding the β‐subunit of mouse β‐hexosaminidase
Author(s) -
Bapat Bharati,
Ethier Marguerite,
Neote Kuldeep,
Mahuran Don,
Gravel Roy A.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80199-6
Subject(s) - complementary dna , peptide sequence , signal peptide , microbiology and biotechnology , biology , amino acid , cdna library , open reading frame , hexosaminidase , protein subunit , nucleic acid sequence , glycosylation , biochemistry , dna , gene , enzyme
A cDNA encoding the prepro‐β‐polypeptide of mouse β‐hexosaminidase (Hex) was isolated from a mouse lymphoblast cDNA library. The cDNA contains an open reading frame corresponding to a polypeptide of 536 amino acids which shows 74% homology with the human prepro‐β‐polypeptide. An examination of the amino acid sequence identifies a putative signal peptide and five possible glycosylation sites, two of which are identical to the confirmed glycosylation sites of the human β‐chain. The amino acid sequence also shows a structurally similar though not identical site for internal cleavage responsible for the generation of mature β a ‐ and β b ‐polypeptides.