Limnanthes douglasii lysophosphatidic acid acyltransferases: immunological quantification, acyl selectivity and functional replacement of the Escherichia coli plsC gene
| Autor: | Clare L. Brough, Simon Carnaby, Adrian P. Brown, Antoni R. Slabas, Melissa Brazier |
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| Rok vydání: | 2002 |
| Předmět: |
Mutant
Blotting Western Molecular Sequence Data Biology medicine.disease_cause Biochemistry Isozyme Antibodies Antibody Specificity medicine Escherichia coli Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence chemistry.chemical_classification Immunoassay Plant Stems Escherichia coli Proteins Cell Membrane food and beverages Cell Biology 1-Acylglycerol-3-Phosphate O-Acyltransferase Plants biology.organism_classification Molecular biology Recombinant Proteins Isoenzymes Kinetics Enzyme Membrane protein chemistry Limnanthes douglasii Acyltransferase Acyltransferases Research Article |
| Zdroj: | The Biochemical journal. 364(Pt 3) |
| ISSN: | 0264-6021 |
| Popis: | Antibodies were raised against the two membrane-bound lysophosphatidic acid acyltransferase (LPAAT) enzymes from Limnanthes douglasii (meadowfoam), LAT1 and LAT2, using the predicted soluble portion of each protein as recombinant protein antigens. The antibodies can distinguish between the two acyltransferase proteins and demonstrate that both migrate in an anomalous fashion on SDS/PAGE gels. The antibodies were used to determine that LAT1 is present in both leaf and developing seeds, whereas LAT2 is only detectable in developing seeds later than 22 daf (days after flowering). Both proteins were found exclusively in microsomal fractions and their amount was determined using the recombinant antigens as quantification standards. LAT1 is present at a level of 27 pg/microg of membrane protein in leaf tissue and |
| Databáze: | OpenAIRE |
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