ISOLATION and CHARACTERIZATION OF PEPTIDES PRODUCED BY THE MILD ACID HYDROLYSIS OF BOVINE SUBMAXILLARY MUCIN*
| Autor: | Fred Downs, Ward Pigman |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Dansyl Compounds
chemistry.chemical_classification Alanine Chromatography Hydrolysis Submandibular Gland Mucins Ovine Submaxillary Mucin Peptide General Medicine Tripeptide Hydrogen-Ion Concentration Peptide Fragments Amino acid Kinetics chemistry Biochemistry Valine Animals Cattle Amino Acid Sequence Hydrochloric Acid Amino Acids Isoleucine Leucine |
| Zdroj: | International Journal of Protein Research. 2:27-36 |
| ISSN: | 0020-7551 |
| DOI: | 10.1111/j.1399-3011.1970.tb01657.x |
| Popis: | The rate of release of amino acids during partial acid hydrolysis of bovine submaxillary mucin has been studied. A number of di- and tripeptides have been isolated on the amino acid analyzer. Three β-hydroxyamino acid peptides, Thr-Thr-Thr, Ser-Ser, and Thr-Ser have been isolated and account for 12 % of these amino acids in native mucin. A substantial amount of the glycine and alanine has been isolated as dipeptides of serine and threonine with the fihydroxyamino acids in the amino-terminal position. Proline, valine, isoleucine, and leucine seem to be in close association in the peptide core. The same pattern of peptides has been obtained from the partial acid hydrolysis of ovine submaxillary mucin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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