Secretion of active urokinase-type plasminogen activator from the yeast Yarrowia lipolyticaopen access
- Authors
- Ryu, Ho Myoung; Kang, Woo Kyu; Kang, Hyun Ah; Kim, Jeong-Yoon
- Issue Date
- Apr-2003
- Publisher
- Korean Society for Biotechnology and Bioengineering
- Keywords
- Secretion; Urokinase-type plasminogen activator; Yarrowia lipolytica
- Citation
- Biotechnology and Bioprocess Engineering, v.8, no.2, pp 162 - 165
- Pages
- 4
- Journal Title
- Biotechnology and Bioprocess Engineering
- Volume
- 8
- Number
- 2
- Start Page
- 162
- End Page
- 165
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57523
- DOI
- 10.1007/BF02940274
- ISSN
- 1226-8372
1976-3816
- Abstract
- In order to study the secretion of the human urokinase-type plasminogen activator, u-PA, from the yeast Yarrowia lipolytica, three kinds of integrative expression vector were constructed. These vectors differed only in their secretion control regions, pre-, pre-dip- (dipeptide stretch) or pre-dip-pro sequences of the alkaline extracellular protease, which were joined inframe to the human u-PA cDNA. The recombinant Y. lipolytica strains, transformed with the expression vectors, secreted the hyperglycosylated u-PA. A fibrin plate assay of the culture supernatants showed that the hyperglycosylated u-PA proteins could catalyze fibrinolysis, and that the pre-dip sequence was the most efficient secretory signal for the secretion of the u-PA from Y. lipolytica. This result suggests that Y. lipolytica can be developed as a potential host for the production of recombinant human u-PA. ?KSBB.
- Files in This Item
-
- Appears in
Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57523)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.