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Pig tyraminase beta protein coding sequence

A technology of porcine monoamine oxidase and dog monoamine oxidase, which is applied in the field of protein coding sequence, can solve the problem of cloning and obtaining the coding protein sequence of porcine MAO-B gene.

Inactive Publication Date: 2005-12-28
SHANGHAI JIAO TONG UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

But so far no cloning of porcine MAO-B gene coding protein sequence has been found

Method used

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  • Pig tyraminase beta protein coding sequence

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Experimental program
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Effect test

Embodiment 1

[0016] Cloning of porcine MAO-B gene cDNA sequence

[0017] The cDNA cloning process of MAO-B gene is shown in the appendix figure 1 .

[0018] The specific operation method of the experimental method used in the cloning process is as follows:

[0019] 1. Electronic cloning

[0020] Using the human MAO-B gene CDS nucleotide sequence as the information probe, run the BLASTn program in NCBI to search in the pig EST database, and obtain a series of pig EST sequences of different lengths that are highly consistent with the probe, and then these sequences Perform assembly and connection to obtain a long sequence, and then use the obtained long sequence as a probe to perform BLASTn again in the pig EST database to obtain more EST sequences, so that the sequence is extended to both ends, and finally the obtained The sequences were spliced ​​to obtain the complete sequence.

[0021] 2. Biological clone verification

[0022] (1) Isolation

[0023] The 30-day-old Dudu piglets were...

Embodiment 2

[0047] Homology Comparison of Porcine MAO-B Coding Sequence

[0048] Search and obtain human, bovine, mouse and dog MAO-B gene coding protein sequences on GenBank, and sequence it with the SEQ ID NO.1 sequence obtained by the present invention obtained by cloning and sequencing, and perform sequence alignment on the molecular biology software DNAman source comparison. The comparison results showed that the homology between SEQ ID NO.1 sequence and the MAO-B gene CDS sequence of human, bovine, mouse, dog and other species was 92.73%, respectively, and the homology of amino acid sequence was 93.81%.

[0049] The sequences and symbols involved in the present invention are listed as follows:

[0050] Information on SEQ ID NO.1

[0051] Shanghai Jiao Tong University

[0052] Porcine MAO-B protein coding sequence

[0053] 2

[0054] 1

[0055] 2559

[0056] DNA

[0057] pig (sus scrofa)

[0058]

[0059] CDS

[0060] (129)...(1691)

[0061] 1

[0062] cgccctgggc gg...

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Abstract

Hog monoamine oxidase B protein coding sequence is characterized by having nucleotide sequence from 129-1691 bit in SEQ IDNO.1 and monoamine oxidase B protein coding sequence homology 92.73% with human, rat, ox and dog, having amino acid sequence polypeptide in SEQ ID No:1, or its conserved variant polypeptide, or its active fragment, or its active derivative, having monoamine oxidase B amino acid sequence homology 93.81% with human, rat, ox and dog, cloning according MAO-B gene sequence, sequencing, obtaining hog MOA-B cDNA sequence, and homologous comparing for different species CDS sequence of MAO-B gene. It can be used for relation of MAO-gene and hog stress sensitivity and human related stress diseases.

Description

technical field [0001] The invention relates to a protein coding sequence used in the field of biogenetic engineering, especially the protein coding sequence of porcine monoamine oxidase B (MAO-B). Background technique [0002] Monoamine oxidase B (monoamine oxidase B, MAO-B) is a flavin enzyme bound to the outer mitochondrial membrane, which is a key enzyme in the oxidative degradation of several important monoamine neurotransmitters. Monoamines have important functions of nerve activity, blood vessel activity and other vital activities, so monoamine oxidase B plays an important role in the regulation of normal neuroendocrine system activity. Monoamine oxidase (MAO) was first discovered by Hare in 1928. In 1970, according to the specificity of its preferred substrate and inhibitor, MAO was divided into two types, A and B. The preferred substrates of MAO-B are phenylethylamine (PEA) and benzylamine, which are specifically inhibited by deprenyl. [0003] Research on MAO-B ...

Claims

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Application Information

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IPC IPC(8): C12N15/53
Inventor 潘玉春白春艳孟和赵威李婧
Owner SHANGHAI JIAO TONG UNIV
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