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Myofibrillar protein serine phosphorylation level detection method capable of avoiding signal interference

A myofibrillar protein and serine phosphorylation technology, applied in the biological field, can solve the problems of inaccurate detection of myofibrillar protein, high cost, cumbersome operation, etc., and achieve clear bands, small amount of muscle samples, and good repeatability Effect

Active Publication Date: 2017-09-29
INST OF AGRO FOOD SCI & TECH CHINESE ACADEMY OF AGRI SCI
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] Yet another object of the present invention is to provide a method for measuring the level of serine phosphorylation of myofibrillar proteins that avoids signal interference, avoids mutual interference of serine phosphorylation signals between various myofibrillar proteins, and realizes the detection of different myofibrillar proteins by using immunoblotting. The determination of the phosphorylation level of myofibrillar protein solves the problems of inaccurate detection of a certain kind of myofibrillar protein, cumbersome operation and high cost in the existing methods

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  • Myofibrillar protein serine phosphorylation level detection method capable of avoiding signal interference
  • Myofibrillar protein serine phosphorylation level detection method capable of avoiding signal interference
  • Myofibrillar protein serine phosphorylation level detection method capable of avoiding signal interference

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Effect test

Embodiment 1

[0076] a) Take part of the longissimus dorsi myofibrillar protein samples stored at -80°C, and measure the protein concentration by BCA method;

[0077] b) SDS-PAGE electrophoresis: use 7.5%, 10%, 12% separating gel and 4% stacking gel, add 10 μg or 2 μg protein sample to each well of the gel, and the protein marker loading volume is 2 μL. The loading amount of myosin heavy chain and actin with higher content in fibrin is 2.5 μg, and the loading amount of other myofibrillar proteins is 10 μg; for the target protein with a molecular weight greater than or equal to 100KDa, use 7.5% separating gel , for the target protein with a molecular weight higher than 40KDa and less than 100KDa, use 10% separation gel, and for the target protein with molecular weight less than or equal to 40KDa, use 12% separation gel; Stop electrophoresis when the distance from the gel substrate is 0.5 mm;

[0078] c) Western blotting (IB): after the electrophoresis, remove the gel plate, put the gel into...

Embodiment 2

[0084] a) Take part of the longissimus dorsi myofibrillar protein samples stored at -80°C, and measure the protein concentration by BCA method;

[0085] b) SDS-PAGE electrophoresis: use 7.5%, 10%, 12% separating gel and 4% stacking gel, add 10 μg or 2 μg protein sample to each well of the gel, and the protein marker loading volume is 2 μL. The loading amount of myosin heavy chain and actin with higher content in fibrin is 2.5 μg, and the loading amount of other myofibrillar proteins is 10 μg; for the target protein with a molecular weight greater than or equal to 100KDa, use 7.5% separating gel , for the target protein with a molecular weight higher than 40KDa and less than 100KDa, use 10% separation gel, and for the target protein with molecular weight less than or equal to 40KDa, use 12% separation gel; Stop electrophoresis when the distance from the gel substrate is 0.5 mm;

[0086] c) Western blotting (IB): after the electrophoresis, remove the gel plate, put the gel into...

Embodiment 3

[0093] a) Take part of the longissimus dorsi myofibrillar protein samples stored at -80°C, and measure the protein concentration by BCA method;

[0094] b) SDS-PAGE electrophoresis: use 7.5%, 10%, 12% separating gel and 4% stacking gel, add 10 μg or 2 μg protein sample to each well of the gel, and the protein marker loading volume is 2 μL. The loading amount of myosin heavy chain and actin with higher content in fibrin is 2.5 μg, and the loading amount of other myofibrillar proteins is 10 μg; for the target protein with a molecular weight greater than or equal to 100KDa, use 7.5% separating gel , for the target protein with a molecular weight higher than 40KDa and less than 100KDa, use a 10% separating gel, and for a target protein with a molecular weight less than or equal to 40KDa, use a 12% separating gel; there is a blank lane between the protein marker and the sample without loading the sample, and electrophoresis The voltage adopts a constant voltage of 200V, and the ele...

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Abstract

The invention provides a myofibrillar protein serine phosphorylation level detection method capable of avoiding signal interference. The phosphorylation level of different myofibrillar protein serine can be detected in postmortem muscles through a protein immunoblotting technology. Few muscle samples are needed, the operation process is simpler, the repeatability is good, the strip obtained through detection is clear, and the experiment cost is low, so that the method can detect the phosphorylation level of the myofibrillar protein serine in the postmortem muscles efficiently. The method can be used for researching and analyzing biochemical change of myofibrillar protein with serine phosphorylated in sheep bone muscles, and also can be used for physical and biochemical research of muscles of other animals.

Description

technical field [0001] The invention belongs to the field of biotechnology, and in particular relates to a method for measuring the phosphorylation level of myofibrillar protein serine which avoids signal interference. Background technique [0002] Protein phosphorylation modification is an important way to regulate protein structure and function. Current methods on protein phosphorylation levels mainly focus on measuring the overall phosphorylation level. Phosphorylation modifications may occur on serine, threonine, and tyrosine, among which the phosphorylation modification of serine is the most numerous. To study the biochemical changes of myofibrillar protein phosphorylation, and based on the effect of myofibrillar protein phosphorylation on The study of animal muscle physiology and biochemistry is indispensable in scientific research. Although there are specific antibodies against a certain amino acid in the prior art, there are many types of myofibrillar proteins, and ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): G01N33/68
CPCG01N33/68
Inventor 李铮张德权陈丽杜曼婷李欣王振宇侯成立潘腾赵梦雅
Owner INST OF AGRO FOOD SCI & TECH CHINESE ACADEMY OF AGRI SCI
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