Primary study of expression of matrix metalloproteinase-2 in yeast Pichia pastoris

Xiu Yun Ding; Chun Hai Li; Yun Feng Zhu; Li Ya Sun; Chun Hong Yan; Li Xin Zhang; Dong Xiao Feng; Gao Ming Chen

Primary study of expression of matrix metalloproteinase-2 in yeast Pichia pastoris

Xiu Yun Ding, Chun Hai Li, Yun Feng Zhu, Li Ya Sun, Chun Hong Yan, Li Xin Zhang, Dong Xiao Feng, Gao Ming Chen

Research output: Contribution to journal › Article › peer-review

Abstract

Matrix metalloproteinase-2 (MMP-2) plays important role in tumor invasion and metastasis. MMP-2 is expressed in yeast expression system for further studying its function mechanism. The expression sequence of MMP-2 (gelatinase A) have been obtained by PCR amplifying, restriction enzyme cut and sequencing analysis demostrate that the sequence is correct. The expression vector pPIC9/GelA containing gelatinase A sequence is constructed and transformed the yeast Pichia pastoris. The gelatin enzymography demostrate that recombinant protein secreted by transformant yeast is capable of degrading gelatin and the molecular weight of the matrix metalloproteinase-2 is 66 ku in SDS-PAGE.

Original language	English (US)
Pages (from-to)	293-294
Number of pages	2
Journal	Progress in Biochemistry and Biophysics
Volume	26
Issue number	3
State	Published - 1999
Externally published	Yes

Keywords

Expression
Matrix metalloproteinase-2
Pichia pastoris

ASJC Scopus subject areas

Biophysics
Biochemistry

Cite this

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title = "Primary study of expression of matrix metalloproteinase-2 in yeast Pichia pastoris",

abstract = "Matrix metalloproteinase-2 (MMP-2) plays important role in tumor invasion and metastasis. MMP-2 is expressed in yeast expression system for further studying its function mechanism. The expression sequence of MMP-2 (gelatinase A) have been obtained by PCR amplifying, restriction enzyme cut and sequencing analysis demostrate that the sequence is correct. The expression vector pPIC9/GelA containing gelatinase A sequence is constructed and transformed the yeast Pichia pastoris. The gelatin enzymography demostrate that recombinant protein secreted by transformant yeast is capable of degrading gelatin and the molecular weight of the matrix metalloproteinase-2 is 66 ku in SDS-PAGE.",

keywords = "Expression, Matrix metalloproteinase-2, Pichia pastoris",

author = "Ding, {Xiu Yun} and Li, {Chun Hai} and Zhu, {Yun Feng} and Sun, {Li Ya} and Yan, {Chun Hong} and Zhang, {Li Xin} and Feng, {Dong Xiao} and Chen, {Gao Ming}",

year = "1999",

language = "English (US)",

volume = "26",

pages = "293--294",

journal = "Progress in Biochemistry and Biophysics",

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TY - JOUR

T1 - Primary study of expression of matrix metalloproteinase-2 in yeast Pichia pastoris

AU - Ding, Xiu Yun

AU - Li, Chun Hai

AU - Zhu, Yun Feng

AU - Sun, Li Ya

AU - Yan, Chun Hong

AU - Zhang, Li Xin

AU - Feng, Dong Xiao

AU - Chen, Gao Ming

PY - 1999

Y1 - 1999

N2 - Matrix metalloproteinase-2 (MMP-2) plays important role in tumor invasion and metastasis. MMP-2 is expressed in yeast expression system for further studying its function mechanism. The expression sequence of MMP-2 (gelatinase A) have been obtained by PCR amplifying, restriction enzyme cut and sequencing analysis demostrate that the sequence is correct. The expression vector pPIC9/GelA containing gelatinase A sequence is constructed and transformed the yeast Pichia pastoris. The gelatin enzymography demostrate that recombinant protein secreted by transformant yeast is capable of degrading gelatin and the molecular weight of the matrix metalloproteinase-2 is 66 ku in SDS-PAGE.

AB - Matrix metalloproteinase-2 (MMP-2) plays important role in tumor invasion and metastasis. MMP-2 is expressed in yeast expression system for further studying its function mechanism. The expression sequence of MMP-2 (gelatinase A) have been obtained by PCR amplifying, restriction enzyme cut and sequencing analysis demostrate that the sequence is correct. The expression vector pPIC9/GelA containing gelatinase A sequence is constructed and transformed the yeast Pichia pastoris. The gelatin enzymography demostrate that recombinant protein secreted by transformant yeast is capable of degrading gelatin and the molecular weight of the matrix metalloproteinase-2 is 66 ku in SDS-PAGE.

KW - Expression

KW - Matrix metalloproteinase-2

KW - Pichia pastoris

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SN - 1000-3282

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ER -

Primary study of expression of matrix metalloproteinase-2 in yeast Pichia pastoris

Abstract

Keywords

ASJC Scopus subject areas

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