Purification and partial characterization of rat factor D
| Autor: | C J Campbell, Gerardo Turcatti, B C Baker, C J Grinham |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Glycosylation
Molecular Sequence Data Size-exclusion chromatography enzyme purification complement factor d Biochemistry Mice chemistry.chemical_compound Complement Factor D Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence enzyme analysis chemistry.chemical_classification biology Hydrolysis Serine Endopeptidases Cell Biology Molecular biology Rats Amino acid Enzyme chemistry Concanavalin A biology.protein Electrophoresis Polyacrylamide Gel Factor D Sequence Alignment Research Article |
| Zdroj: | Biochemical Journal. 279:775-779 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2790775 |
| Popis: | Rat factor D has been purified to homogeneity (10,559-fold) from serum by chromatography on CM-Sepharose Fast Flow, phenyl-Sepharose CL-4B and Mono S and has been shown to resemble its human and mouse counterparts both in substrate specificity and in its susceptibility to inhibition by the organophosphorous inhibitor di-isopropylfluorophosphate. The rat enzyme, however, is heavily glycosylated and binds to wheat-germ lectin-Sepharose 6MB and 5-hydroxytryptamine-agarose, but not to concanavalin A-Sepharose 4B. All of the carbohydrate chains are N-linked. Enzymic removal of this carbohydrate decreased the Mr by approx. 15,000. The deglycosylated rat enzyme had the same mobility as native human factor D on SDS/PAGE, corresponding to an Mr of 24,500. N-Terminal sequence analysis of the first 30 amino acids of rat factor D highlighted the sequence similarity with human factor D (greater than 76%) and, in particular, with mouse adipsin (greater than 93%). |
| Databáze: | OpenAIRE |
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