The Solubilization of Unheated Cattle Achilles Tendon with Actinidin under Neutral and Acidic Conditions
| Autor: | Tadao Hasegawa, Masaru Hosaka, Masahiro Wada, Yuuji Kobayashi, Ryoji Nakazawa |
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| Rok vydání: | 2004 |
| Předmět: |
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Gel electrophoresis chemistry.chemical_classification Achilles tendon biology General Chemical Engineering Protein subunit Peptide Anatomy Industrial and Manufacturing Engineering Tendon Hydroxyproline chemistry.chemical_compound medicine.anatomical_structure chemistry Biochemistry Solubilization medicine biology.protein Elastin Food Science Biotechnology |
| Zdroj: | Food Science and Technology Research. 10:35-37 |
| ISSN: | 1881-3984 1344-6606 |
| Popis: | The solubilization of cattle achilles tendon with actinidin was investigated under neutral and acidic conditions. 1.43 to 1.92 and 0.97 to 3.19% of collagen were solubilized by treating the cattle achilles tendon with actinidin at 20°C at pH 6.0 and 3.3, respectively. Furthermore, SDS-polyacrylamide gel electrophoresis of reaction mixtures with actinidin demonstrated that actinidin degraded the tendon into collagen subunit chain, β- and α-chain and peptide fragments of various sizes at 20°C at pH 6.0 and 3.3. These results indicated that actinidin could solubilize the insoluble collagen in unheated cattle achilles tendon at 20°C at pH 6.0 and 3.3 and that a large proportion of the resulting peptide fragments by actinidin seemed to be actinidin digests against elastin with a small contribution of hydroxyproline. |
| Databáze: | OpenAIRE |
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