Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase
In this paper we describe isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase (DAP-AT). The enzyme was extracted from rabbit Harderian gland peroxisomes and isolated as a trimeric complex by sucrose density gradient centrifugation. From peptide sequences match...
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| Main Authors: | , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
December 29, 1997
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| In: |
FEBS letters
Year: 1997, Volume: 420, Issue: 2/3, Pages: 205-211 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/S0014-5793(97)01495-6 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/S0014-5793(97)01495-6 Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1016/S0014-5793%2897%2901495-6 
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| Author Notes: | Thanh-Phuong Thai, Hans Heid, Hans-Richard Rackwitz, Andreas Hunziker, Karin Gorgas, Wilhelm W Just |
| Summary: | In this paper we describe isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase (DAP-AT). The enzyme was extracted from rabbit Harderian gland peroxisomes and isolated as a trimeric complex by sucrose density gradient centrifugation. From peptide sequences matching EST-clones were obtained which allowed cloning and sequencing of the cDNA from a human cDNA library. The nucleotide-derived amino acid sequence revealed a protein consisting of 680 amino acid residues of molecular mass 77 187 containing a C-terminal type 1 peroxisomal targeting signal. Monospecific antibodies raised against this polypeptide efficiently immunoprecipitated DAP-AT activity from solubilized peroxisomal preparations, thus demonstrating that the cloned cDNA codes for DAP-AT. |
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| Item Description: | Gesehen am 22.04.2025 |
| Physical Description: | Online Resource |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/S0014-5793(97)01495-6 |