Evidence for post-transcriptional modification of human salivary amylase (Amy1) isozymes
| Autor: | Merritt Ad, Robert C. Karn, Newell Rc, Shulkin Jd |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
chemistry.chemical_classification
Saliva Sublingual gland General Medicine Biology Biochemistry Isozyme Molecular biology Submandibular gland Parotid gland Gene product stomatognathic diseases medicine.anatomical_structure Enzyme stomatognathic system chemistry Genetics medicine biology.protein Amylase Molecular Biology Ecology Evolution Behavior and Systematics |
| Zdroj: | Biochemical Genetics. 10:341-350 |
| ISSN: | 1573-4927 0006-2928 |
| Popis: | Human parotid salivary amylase (Amy1) isozymes may be separated into two families: (1) one of higher molecular weight and slower electrophoretic mobility, odds, and (2) the other of lower molecular weight and faster electrophoretic mobility, evens. An enzyme has been detected in whole saliva, and also partially purified from human oral bacterial flora, which converts the isoamylases from odds to evens. No similar modifying activity was detected in parotid saliva or submandibular and sublingual salivas. A model is presented which explains the multiple isozymes of salivary amylase by post-transcriptional modification of a single gene product. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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