BMP-4 Extraction from Extracellular Matrix and Analysis of Heparin-Binding Properties.
BMP-4 Extraction from Extracellular Matrix and Analysis of Heparin-Binding Properties.
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DOI:
10.1007/s12033-021-00403-x
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发表时间:
2022-03
影响因子:
2.6
通讯作者:
Martinez-Hackert E
中科院分区:
文献类型:
--
作者:
Aykul S;Maust J;Martinez-Hackert E
Recombinant human BMP-4 growth factor (GF) has significant commercial potential as therapeutic for regenerating bone and as cell culture supplement. However, its commercial utility has been limited as large-scale attempts to express and purify human BMP-4 GF have proved challenging. We have established a novel approach to obtain significant quantities of pure and bioactive BMP-4 GF from Chinese hamster ovary cell cultures by extracting the GF moiety from the extracellular matrix or cell pellet fraction. This approach increased yields approximately one 100-fold over BMP-4 GF purified from CM. The molecular activities of the two fractions are indistinguishable. We further analyzed binding of BMP-4 GF to the proteoglycan Heparin and showed that an N-terminal basic sequence is essential for this interaction. Taken together, these results provide novel insights into the purification, localization, and Heparin binding of human BMP-4 that have implications for its bioprocessing and biological function.
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DOI:
10.1016/j.btre.2018.e00249
发表时间:
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期刊:
Biotechnology reports (Amsterdam, Netherlands)
影响因子:
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DOI:
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发表时间:
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期刊:
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影响因子:
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