W. Wong, Edward Lam R.C. Huang, R. Wong, C. Morris, J. Hackett
{"title":"Applications, and Efficient Large-Scale Production, of Recombinant Human Epidermal Growth Factor","authors":"W. Wong, Edward Lam R.C. Huang, R. Wong, C. Morris, J. Hackett","doi":"10.1080/02648725.2001.10648008","DOIUrl":null,"url":null,"abstract":"Human epidermal growth factor (EOF) is a small polypeptide of molecular weight 6201 Daltons, with 53 amino acid residues. Since its discovery by Cohen (1962) (an achievement subsequently honoured by the award of the 1986 Nobel Prize in Medicine), all aspects of EGF biology have attracted intense research interest. A search of the OvidTM Biological Abstract database (1991-1999), with the search phrase 'epidennaI growth factor', and restriction to the English language, yielded 10,614 hits. In the first part of this article, we review some papers from the interval ]995-1999.. which have been chosen to show actual or potential uses of EGF, mainly in various facets of human health care. In choosing papers for review in this section, space constraints have compelled us to ignore many fine research contributions which dealt for example, with aspects of the interaction of EGF with its receptor, or which detail the influence of EGF upon various signal transduction pathways within the cell. The review section concludes with the suggestion that many potential applications ofEGF are thwarted by the relative unavailabiIity of large aJTIounts of purifiedt biologically active t chemically authentic EGF. In the next section~ then, we review earlier efforts to produce recombinant EGF in quantity, and subsequently focus on more recent work in our laboratory, which has resulted in a fast, reliable method for the production of gram quantities of purified human EGF which is chemically identical to the natural material and exhibits full biological activity. We conclude that the availability of EGF in large quantities will be of practical use to patients and their","PeriodicalId":8931,"journal":{"name":"Biotechnology and Genetic Engineering Reviews","volume":"85 1","pages":"51 - 71"},"PeriodicalIF":0.0000,"publicationDate":"2001-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"23","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biotechnology and Genetic Engineering Reviews","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/02648725.2001.10648008","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 23
Abstract
Human epidermal growth factor (EOF) is a small polypeptide of molecular weight 6201 Daltons, with 53 amino acid residues. Since its discovery by Cohen (1962) (an achievement subsequently honoured by the award of the 1986 Nobel Prize in Medicine), all aspects of EGF biology have attracted intense research interest. A search of the OvidTM Biological Abstract database (1991-1999), with the search phrase 'epidennaI growth factor', and restriction to the English language, yielded 10,614 hits. In the first part of this article, we review some papers from the interval ]995-1999.. which have been chosen to show actual or potential uses of EGF, mainly in various facets of human health care. In choosing papers for review in this section, space constraints have compelled us to ignore many fine research contributions which dealt for example, with aspects of the interaction of EGF with its receptor, or which detail the influence of EGF upon various signal transduction pathways within the cell. The review section concludes with the suggestion that many potential applications ofEGF are thwarted by the relative unavailabiIity of large aJTIounts of purifiedt biologically active t chemically authentic EGF. In the next section~ then, we review earlier efforts to produce recombinant EGF in quantity, and subsequently focus on more recent work in our laboratory, which has resulted in a fast, reliable method for the production of gram quantities of purified human EGF which is chemically identical to the natural material and exhibits full biological activity. We conclude that the availability of EGF in large quantities will be of practical use to patients and their