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Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B)
- Source :
- Biochemical and biophysical research communications. 163(3)
- Publication Year :
- 1989
-
Abstract
- In the process of molecular cloning of cDNA for proteins associated with a purified human placental sialidase fraction, we discovered one of the proteins with apparent molecular weight of 46 kDa is in reality alpha-N-acetylgalactosaminidase. The full length cDNA, pcD-HS1204, codes for 358 amino acids with the first 17 residues representing a putative signal peptide. The predicted amino acid sequence shows striking homology with human alpha-galactosidase A and yeast alpha-galactosidase. The substrate specificities as well as the behavior of the 46 kDa protein on hydroxylapatite chromatography confirmed that the 46 kDa protein is in reality alpha-N-acetylgalactosaminidase.
- Subjects :
- Signal peptide
Placenta
Molecular Sequence Data
Biophysics
Molecular cloning
Biology
Sialidase
Biochemistry
Homology (biology)
alpha-N-Acetylgalactosaminidase
Pregnancy
Complementary DNA
Humans
Amino Acid Sequence
Cloning, Molecular
Molecular Biology
Peptide sequence
chemistry.chemical_classification
Chromatography
Base Sequence
Nucleic acid sequence
Cell Biology
DNA
Molecular biology
Amino acid
Molecular Weight
Kinetics
Durapatite
Hexosaminidases
chemistry
Female
Hydroxyapatites
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 163
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....3d43044909f51947f034641f8de671e5