Purification and immunochemistry of a soluble matrix protein of the chicken eggshell (ovocleidin 17)
| Autor: | V. Hill, C. P. W. Tsang, M. Courtney, M. T. Hincke, Roberto M. Narbaitz |
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| Rok vydání: | 1995 |
| Předmět: |
Endocrinology
Diabetes and Metabolism Blotting Western Molecular Sequence Data Matrix (biology) Egg Shell Endocrinology Immunochemistry medicine Animals Orthopedics and Sports Medicine Amino Acid Sequence Amino Acids Eggshell Tubular gland Peptide sequence Polyacrylamide gel electrophoresis Viral matrix protein Chemistry Egg Proteins Chromatography Ion Exchange Molecular biology Molecular Weight Blot medicine.anatomical_structure Biochemistry Electrophoresis Polyacrylamide Gel Chickens |
| Zdroj: | Calcified Tissue International. 56:578-583 |
| ISSN: | 1432-0827 0171-967X |
| DOI: | 10.1007/bf00298593 |
| Popis: | The protein components of biomineralized structures (matrix proteins) are believed to modulate crystal nucleation and growth, and thereby influence the shape and strength of the final structure. The chicken eggshell contains a complex array of distinct matrix proteins. The most abundant of these was purified to homogeneity by a combination of anionic exchange and hydroxyapatite chromatographies. Antibodies to this protein were raised in rabbit, and utilized for Western blotting and immunohistochemistry. These studies indicated that the 17 kDa antigen (ovocleidin 17, OC-17) is found in the shell gland mucosa, and that only the tubular gland cells were positive. Immunohistochemistry with decalcified shell indicated that OC-17 is uniformly distributed throughout the shell matrix, but concentrated in the mammillary bodies. Our results indicate that this protein is secreted during shell formation and becomes incorporated into this structure. It may therefore play a role in the crystallization process and influence the properties of the resulting eggshell. |
| Databáze: | OpenAIRE |
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