Two-step purification strategy for enhanced recovery of recombinant hepatitis B surface antigen fromPichia pastoris-Reference-Cited by-同舟云学术

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Two-step purification strategy for enhanced recovery of recombinant hepatitis B surface antigen fromPichia pastoris

Published:2016-01-15 Issue:5 Volume:51 Page:816-829
ISSN:0149-6395
Container-title:Separation Science and Technology
language:en
Short-container-title:Separation Science and Technology

Author:

Tam Yew Joon,Zeenathul Nazariah Allaudin,Rezaei Morvarid Akhavan,Mohd Azmi Mohd Lila,Bahaman Abdul Rani,Lo Sewn Cen,Tan Joo Shun,Hani Homayoun

Funder

Ministry of Science and Technology of Malaysia (MOSTI)

Publisher

Informa UK Limited

Subject

Filtration and Separation,Process Chemistry and Technology,General Chemical Engineering,General Chemistry

Link

http://www.tandfonline.com/doi/pdf/10.1080/01496395.2015.1135949

Reference49 articles.

1. Virus-like particle production with yeast: ultrastructural and immunocytochemical insights into Pichia pastoris producing high levels of the Hepatitis B surface antigen

2. High–Level Expression and Efficient Assembly of Hepatitis B Surface Antigen in the Methylotrophic Yeast, Pichia Pastoris

3. Expression of Hepatitis B Virus S Gene in Pichia pastoris and Application of the Product for Detection of Anti-HBs Antibody

4. Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris

5. A highly efficient integrated chromatographic procedure for the purification of recombinant hepatitis B surface antigen from Hansenula polymorpha

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Purification of high-temperature resistant polyethylene terephthalate (PET) hydrolase by simple heating protocol;Process Biochemistry;2022-03

2. Butylated hydroxytoluene protects bull sperm surface protein-P25b in different extenders following cryopreservation;April-2020;2020

3. A novel application of ion exchange chromatography in recombinant hepatitis B vaccine downstream processing: Improving recombinant HBsAg homogeneity by removing associated aggregates;Journal of Chromatography B;2019-04

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