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Determination of the bands of four common animal collagens by SDS-PAGE electrophoresis and the comparative study of their protein functional regions

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DOI: 10.23977/medsc.2023.040601 | Downloads: 22 | Views: 379

Author(s)

Yibo Jiang 1, Linlin Zheng 1, Linlu Lin 1, Shan Lin 1

Affiliation(s)

1 Department of Biomedical Engineering, Shenzhen People's Hospital, Shenzhen, 518020, Guangdong, China

Corresponding Author

Yibo Jiang

ABSTRACT

Collagen is the most abundant protein in animals, which is widely distributed in all kinds of animals, and its composition and evolution is very complex. In this study, SDS-PAGE protein electrophoresis was used to determine the changes of electrophoretic bands of collagen extracted by enzymatic hydrolysis from pigs, cattle, fish and rats, and the results of electrophoretic hydrolysis are summarized below. Hydrolysis from pigs, cattle, fish and rats, and the results of electrophoretic bands were classified and sorted out. Using the different characteristics and proportion data of collagen electrophoretic bands of four kinds of animals, the characteristic bands were analyzed, and the Using the different characteristics and proportion data of collagen electrophoretic bands of four kinds of animals, the characteristic bands were analyzed, and the functional region analysis and prediction tool of SMART protein was used. The relevant research results provide a reference for clarifying the characteristics of collagen evolved in different animals and for the establishment of its determination methodology, and for the determination of collagen in different animals. The relevant research results provide a reference for clarifying the characteristics of collagen evolved in different animals and for the establishment of its determination methodology, and provide experimental data and scientific basis for the development of different types of collagen medical products.

KEYWORDS

Electrophoresis; collagen; SMART; evolution

CITE THIS PAPER

Yibo Jiang, Linlin Zheng, Linlu Lin, Shan Lin, Determination of the bands of four common animal collagens by SDS-PAGE electrophoresis and the comparative study of their protein functional regions. MEDS Clinical Medicine (2023) Vol. 4: 1-12. DOI: http://dx.doi.org/10.23977/medsc.2023.040601.

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