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A New Method for Determining the Integrity of Type I Collagen Triple Helix Structure

A technology for structural integrity and collagen, which is applied in the field of judging the integrity of type I collagen triple helix, can solve the problems of collagen triple helix structure damage and affect biological activity, etc., to achieve quantitative analysis, good reproducibility, Simple operation effect

Active Publication Date: 2021-07-20
HUAIHAI INST OF TECH +1
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the triple helix structure of collagen is easily affected by the processing environment and other external conditions, such as external temperature, pressure, and chemical reagents introduced during processing and production. These factors will lead to the destruction of the triple helix structure of collagen, affecting its biological activity

Method used

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  • A New Method for Determining the Integrity of Type I Collagen Triple Helix Structure
  • A New Method for Determining the Integrity of Type I Collagen Triple Helix Structure
  • A New Method for Determining the Integrity of Type I Collagen Triple Helix Structure

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0072] (1) Take the collagen sample of aquatic carp skin to be tested, add pre-cooled 0.5M acetic acid solution, dissolve it at 10°C and divide it into tubes A and B, and add an appropriate amount of pepsin;

[0073] (2) Tube A is always in a water bath at 10°C, and tube B is placed in a water bath at 40°C;

[0074] (3) At the set time, draw samples from tubes A and B into tubes A1 and B1 respectively;

[0075] (4) Place tubes A1 and B1 in an ice water bath quickly, and add pepsin inhibitor (Pepstatin);

[0076] (5) Repeat the operation from steps (3) to (4) and change the set time. A1 and B1 are obtained at 0 minutes, A2 and B2 at 30 minutes, A3 and B3 at 1 hour, and A4 and B4 at 2 hours , get A5, B5 at 3h, A6, B6 at 5h;

[0077] (6) Prepare electrophoresis samples from the obtained A1-6 and B1-6 samples, such as figure 1 and 2 as shown, figure 1 The 6 bands shown in are respectively A1, A2, A3, A4, A5, A6, figure 2 The six bands shown in are B1, B2, B3, B4, B5, and B6...

Embodiment 2

[0083] (1) Take the collagen-rich animal tissue pigskin collagen sample to be tested, add pre-cooled 0.1M acetic acid solution, dissolve at 5°C and divide into tubes A and B, and add appropriate amount of pepsin;

[0084] (2) Tube A is always in a water bath at 0°C, and tube B is placed in a water bath at 80°C;

[0085] (3) At the set time, draw samples from tubes A and B into tubes A1 and B1 respectively;

[0086](4) Place tubes A1 and B1 in an ice water bath quickly, and add pepsin inhibitor (Pepstatin);

[0087] (5) Repeat the operation from steps (3) to (4) and change the set time. A1 and B1 are obtained at 0 minutes, A2 and B2 at 30 minutes, A3 and B3 at 1 hour, and A4 and B4 at 2 hours , get A5, B5 at 3h, A6, B6 at 5h;

[0088] (6) Prepare electrophoresis samples from the obtained A1-6 and B1-6 samples; image 3 and 4 as shown, image 3 The 6 bands shown in are respectively A1, A2, A3, A4, A5, A6, Figure 4 The 6 bands shown in are B1, B2, B3, B4, B5, B6 respective...

Embodiment 3

[0094] (1) Take the beef tendon collagen sample of animal tissue rich in collagen to be tested, add pre-cooled 0.5M acetic acid solution, dissolve at 0°C, and divide into tubes A and B, and add appropriate amount of pepsin;

[0095] (2) Tube A is always in a water bath at 10°C, and tube B is placed in a water bath at 70°C;

[0096] (3) At the set time, draw samples from tubes A and B into tubes A1 and B1 respectively;

[0097] (4) Place tubes A1 and B1 in an ice water bath quickly, and add pepsin inhibitor (Pepstatin);

[0098] (5) Repeat the operation from steps (3) to (4) and change the set time. A1 and B1 are obtained at 0 minutes, A2 and B2 at 30 minutes, A3 and B3 at 1 hour, and A4 and B4 at 2 hours , get A5, B5 at 3h, A6, B6 at 5h;

[0099] (6) Prepare electrophoresis samples from the obtained A1-6 and B1-6 samples; Figure 5 and 6 as shown, image 3 The 6 bands shown in are respectively A1, A2, A3, A4, A5, A6, Figure 4 The 6 bands shown in are B1, B2, B3, B4, B5,...

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Abstract

The invention discloses a new method for judging the integrity of the triple helix structure of type I collagen, which belongs to the technical field of biological detection. Lost or partially lost collagen is easily decomposed into small molecular weight peptides by proteases. The decomposed peptides can be visualized and analyzed by SDS-PAGE. The more decomposed peptides, it indicates the triple helix structure of the collagen sample. The worse the integrity; on the contrary, if SDS-PAGE does not appear to be decomposed small molecular peptides, it shows that the integrity of the triple helix structure of the collagen sample is better; the present invention can also be scanned by gel electrophoresis imaging system or thin layer The system quantitatively detects the dimeric protein in the collagen sample, thereby calculating the retention rate of the triple helix structure of the collagen sample, which makes up for the deficiency of qualitative detection; the integrity of the collagen triple helix structure is judged by this method, and the results are repeated. It has good reproducibility, strong specificity and simple operation, and can be used for the detection of collagen products.

Description

technical field [0001] The invention belongs to the technical field of biological detection, and in particular relates to a method for judging the integrity of the triple helix of type I collagen and calculating the retention rate of the triple helix structure. Background technique [0002] Type I collagen is a right-handed superhelical fibrous protein formed by three peptide chains, and is an important protein in animal connective tissue. Because of the high content of collagen in connective tissue, it has certain structural and mechanical properties, such as tensile strength, tension, elasticity, etc., to support and protect the body. Due to the many excellent properties of collagen, this kind of biopolymer compound has a wide range of uses, covering medicine, chemical industry, food and other fields, among which the application of biomaterials and medicine is the main topic of current research. [0003] The different uses of collagen products mainly depend on the prepara...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): G01N27/447C12P21/06
Inventor 段蕊张俊杰苏东
Owner HUAIHAI INST OF TECH
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