Molecular characterization of glutamic acid/glutamine-rich secretory proteins from rat submandibular glands
| Autor: | D P Dickinson, K W Gross, Lawrence A. Tabak, G S Bedi, L Mirels |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
chemistry.chemical_classification
Nucleic acid sequence Cell Biology Glutamic acid Biology Biochemistry Molecular biology Submandibular gland Amino acid Glutamine medicine.anatomical_structure Secretory protein stomatognathic system chemistry Tandem repeat medicine Molecular Biology Peptide sequence hormones hormone substitutes and hormone antagonists |
| Zdroj: | Journal of Biological Chemistry. 262:7289-7297 |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(18)48235-x |
| Popis: | A family of abundant rat submandibular gland secretory proteins has been identified in glandular extracts and characterized. By amino acid analysis these proteins contain approximately 35% glutamic acid and glutamine plus 14% proline. They have therefore been named "Glx-rich proteins" (GRP). Plasmids containing cDNAs for a GRP have been isolated from a cDNA library prepared from rat submandibular gland poly(A)+RNA. The nucleotide sequence of these cDNAs have been determined. Approximately half of the protein coding sequence is composed of a 23-residue tandem repeat which is repeated five times. The first four repeats are highly conserved at both the nucleotide and amino acid level and consist of the prototype sequence: Asn-Gln-Glu-Pro-Pro-Ala-Thr-Ser-Gly-Ser-Glu-Glu-Glu-Gln-Gln-Gln-Gln-Glu- Pro-Thr-Gln-Ala-Glu. The expression of GRP appears to be specific to the submandibular gland. In vitro assays demonstrate that the GRP have a marked affinity for hydroxyapatite. This suggests that GRP may play a role in the formation of the protective acquired pellicle at the saliva-tooth interface. |
| Databáze: | OpenAIRE |
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