Chloroplast and cytoplasmic enzymes: Isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases
| Autor: | Louise E. Anderson, Robert L. Heinrikson, Paul W. Morris, Heidi A. Zurcher-Neely, Kuldeep Razdan |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Cytoplasm
Chloroplasts Molecular Sequence Data Restriction Mapping Biophysics Fructose-bisphosphate aldolase Biology Biochemistry Isozyme Species Specificity Molecular evolution Fructose-Bisphosphate Aldolase Complementary DNA Amino Acid Sequence Cloning Molecular Molecular Biology Genetics Plants Medicinal Base Sequence cDNA library Aldolase A Nucleic acid sequence food and beverages Fabaceae DNA Chloroplast biology.protein Sequence Alignment |
| Zdroj: | Archives of Biochemistry and Biophysics. 298:192-197 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(92)90112-a |
| Popis: | Two cDNAs which correspond to two very similar Class I aldolases have been isolated from a pea (Pisum sativum L.) cDNA library. With the exception of one codon they match the experimentally determined N-terminal sequence of a pea chloroplast aldolase. The deduced C-terminal sequence of one of these clones is unique among Class I aldolases. The deduced C-terminus of the other is more like the C-terminus of other eucaryotic Class I aldolases. Comparisons of sequence homology suggest that the pea chloroplast isozymes are only marginally more closely related to the anaerobically induced plant aldolases than to aldolases from animals. |
| Databáze: | OpenAIRE |
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