A simple purification procedure of biologically active recombinant human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture

Niti Sharma; Seung Moon Park; Tae Ho Kwon; Dae Hyuk Kim; Moon Sik Yang

doi:10.1007/BF02933480

A simple purification procedure of biologically active recombinant human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture

Niti Sharma
, Seung Moon Park
, Tae Ho Kwon
, Dae Hyuk Kim
, Moon Sik Yang^*

^*Corresponding author for this work

Jeonbuk National University

Research output: Contribution to journal › Journal article › peer-review

5 Scopus citations

Abstract

A simple purification procedure of bioactive human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture has previously been described. In this study the protein was purified to apparent homogeneity with an overall yield of 80.1% by ammonium sulfate precipitation and a single chromatographic step involving FPLC-anion exchange chromatography. The purified hGM-CSF revealed at least five glycosylated forms ranging from 21.5∼29 kDa, and its biological activity was independent of the glycosylation pattern. This is the first purification report of recombinant hGM-CSF to apparent homogeneity from rice cell suspension cultures.

Original language	English
Pages (from-to)	423-427
Number of pages	5
Journal	Biotechnology and Bioprocess Engineering
Volume	9
Issue number	6
DOIs	https://doi.org/10.1007/BF02933480
State	Published - 2004

Keywords

Glycosylation
hGM-CSF
Protein purification
Rice cell suspension culture

Quacquarelli Symonds(QS) Subject Topics

Engineering - Chemical
Biological Sciences

Access to Document

10.1007/BF02933480

Cite this

@article{35bab5c242d9405daee3577f75bb9e25,

title = "A simple purification procedure of biologically active recombinant human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture",

abstract = "A simple purification procedure of bioactive human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture has previously been described. In this study the protein was purified to apparent homogeneity with an overall yield of 80.1\% by ammonium sulfate precipitation and a single chromatographic step involving FPLC-anion exchange chromatography. The purified hGM-CSF revealed at least five glycosylated forms ranging from 21.5∼29 kDa, and its biological activity was independent of the glycosylation pattern. This is the first purification report of recombinant hGM-CSF to apparent homogeneity from rice cell suspension cultures.",

keywords = "Glycosylation, hGM-CSF, Protein purification, Rice cell suspension culture",

author = "Niti Sharma and Park, \{Seung Moon\} and Kwon, \{Tae Ho\} and Kim, \{Dae Hyuk\} and Yang, \{Moon Sik\}",

year = "2004",

doi = "10.1007/BF02933480",

language = "English",

volume = "9",

pages = "423--427",

journal = "Biotechnology and Bioprocess Engineering",

issn = "1226-8372",

number = "6",

}

A simple purification procedure of biologically active recombinant human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture. / Sharma, Niti; Park, Seung Moon; Kwon, Tae Ho et al.
In: Biotechnology and Bioprocess Engineering, Vol. 9, No. 6, 2004, p. 423-427.

Research output: Contribution to journal › Journal article › peer-review

TY - JOUR

T1 - A simple purification procedure of biologically active recombinant human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture

AU - Sharma, Niti

AU - Park, Seung Moon

AU - Kwon, Tae Ho

AU - Kim, Dae Hyuk

AU - Yang, Moon Sik

PY - 2004

Y1 - 2004

N2 - A simple purification procedure of bioactive human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture has previously been described. In this study the protein was purified to apparent homogeneity with an overall yield of 80.1% by ammonium sulfate precipitation and a single chromatographic step involving FPLC-anion exchange chromatography. The purified hGM-CSF revealed at least five glycosylated forms ranging from 21.5∼29 kDa, and its biological activity was independent of the glycosylation pattern. This is the first purification report of recombinant hGM-CSF to apparent homogeneity from rice cell suspension cultures.

AB - A simple purification procedure of bioactive human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture has previously been described. In this study the protein was purified to apparent homogeneity with an overall yield of 80.1% by ammonium sulfate precipitation and a single chromatographic step involving FPLC-anion exchange chromatography. The purified hGM-CSF revealed at least five glycosylated forms ranging from 21.5∼29 kDa, and its biological activity was independent of the glycosylation pattern. This is the first purification report of recombinant hGM-CSF to apparent homogeneity from rice cell suspension cultures.

KW - Glycosylation

KW - hGM-CSF

KW - Protein purification

KW - Rice cell suspension culture

UR - https://www.scopus.com/pages/publications/21644434274

U2 - 10.1007/BF02933480

DO - 10.1007/BF02933480

M3 - Journal article

AN - SCOPUS:21644434274

SN - 1226-8372

VL - 9

SP - 423

EP - 427

JO - Biotechnology and Bioprocess Engineering

JF - Biotechnology and Bioprocess Engineering

IS - 6

ER -

A simple purification procedure of biologically active recombinant human granulocyte macrophage colony stimulating factor (hGM-CSF) secreted in rice cell suspension culture

Abstract

Keywords

Quacquarelli Symonds(QS) Subject Topics

Access to Document

Other files and links

Fingerprint

Cite this