Purification of Recombinant Human Epidermal Growth Factor Secreted from the Methylotrophic Yeast Hansenula polymorpha

Heo, Joo Hyung; Won, Hye Soon; Kang, Hyun Ah; Rhee, Shin Hyung; Chung, Bong Hyun

doi:10.1006/prep.2001.1527

Cited by 21 publications

(11 citation statements)

References 16 publications

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“…The porcine EGF (pEGF) gene, which is found similar to the EGF gene in other mammals, has been produced as a fusion protein in S. cerevisiae (Pascall et al, 1991). Either human EGF (hEGF) or mouse (mEGF) has been expressed in Escherichia coli (Smith et al, 1982;Oka et al, 1985;Tong et al, 2001), Bacillus brevis (Yamagata et al, 1989), and yeast (Clare et al, 1991;Heo et al, 2002). Clare et al (1991) constructed the mEGF gene with a prepro-leader sequence derived from the mating pheromone, a-factor and showed that when integrated into Pichia pastoris strains, the mEGF gene can efficiently secrete the biological activity of recombinant mEGF protein.…”

Section: Introductionmentioning

confidence: 99%

Expression of porcine epidermal growth factor in Pichia pastoris and its biology activity in early-weaned piglets

et al. 2006

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Section: Introductionmentioning

confidence: 99%

Expression of porcine epidermal growth factor in Pichia pastoris and its biology activity in early-weaned piglets

et al. 2006

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“…As proteases cut in loop or accessible structures preferably (Yoo et al 2001;Heo et al 2002), one could speculate that the region around position 44-45 would not be in a helical conformation as predicted, but would rather be in unordered or flexible conformation. This would be in agreement with the helical content of MB1Trp, which is lower than expected per design (55% vs 75%).…”

Section: Discussionmentioning

confidence: 92%

Controlling proteolytic degradation of the methionine enriched MB-1Trp protein

Beauregard¹,

Sasseville²,

St-Louis³

et al. 2004

Electro Journal of Biotech

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Financial support: This work was supported by grants from CORPAQ (Gouvernement du Québec) and NSERC (Canada) awarded to M.B.Keywords: agro-biotechnology, essential amino acids, protein design, protein engineering, proteolysis. Protein design is currently used for the creation of new proteins with desirable traits, which include a superior nutritional value. One of the challenges of protein design in this area is to achieve the production of stable native-like proteins that resist the proteolytic pressure of the organism used for its production (the bioreactor). Abbreviations *Corresponding authorWe report here the identification of a specific peptide bond sensitive to E. coli proteolysis in the designer protein MB-1Trp. In an attempt to reduce proteolysis, we have created a MB-1TrpHis gene library in which the two amino acids surrounding the peptide bond, N44 and L45, were randomized using degenerated

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“…A major drawback of the fusion approach is the formation of rEGF as variants possessing different peptide lengths (Table 1) [11][12][13][14][15][16][17][18][19][20][21][22]. Moreover, the EGF derivatives were commonly shown to exhibit lower levels of bioactivity and stability [17,[22][23][24].…”

Section: Approaches Of Expressing Recombinant Egfmentioning

confidence: 99%

Review Article: Reasons for Underrating the Potential of Human Epidermal Growth Factor in Medical Applications

Wong¹,

Kl²,

Cc³

et al. 2017

JAPLR

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Human epidermal growth factor (EGF) is a functionally versatile polypeptide comprising 53 amino acids (aa). Due to the ability of EGF to stimulate epidermal growth and proliferation, numerous research studies have been conducted to explore its potential applications in cosmetic, skin care and medication. The emergence of recombinant DNA technology has facilitated the production of a great variety of recombinant EGF (rEGF) isoforms. However, increasing evidence supports that rEGF isoforms exhibit different levels of stability and potency. This review discusses how the less bioactive rEGF isoforms may mystify the identity and even the functional properties of authentic rEGF, which shares the same primary structure as native EGF. The identity crisis, the time-consuming, costly and labor-intensive patenting and drug regulatory processes act together to result in underrating the functional applications of authentic rEGF, which have been shown to be effective and safe in promoting treatments of a variety of skin disorders such as diabetic foot ulcers (DFU).

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Purification of Recombinant Human Epidermal Growth Factor Secreted from the Methylotrophic Yeast Hansenula polymorpha

Cited by 21 publications

References 16 publications

Expression of porcine epidermal growth factor in Pichia pastoris and its biology activity in early-weaned piglets

Expression of porcine epidermal growth factor in Pichia pastoris and its biology activity in early-weaned piglets

Controlling proteolytic degradation of the methionine enriched MB-1Trp protein

Review Article: Reasons for Underrating the Potential of Human Epidermal Growth Factor in Medical Applications

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