NDLI: Expression, purification, and lipolytic activity of recombinant human serum albumin fusion proteins with one domain of human growth hormone in Pichia pastoris.

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Expression, purification, and lipolytic activity of recombinant human serum albumin fusion proteins with one domain of human growth hormone in Pichia pastoris.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Furong Wu, Min Liu, Wenhui Shen, Qi Sun, Hongying Chen, Shuqing
Description	Author Affiliation: Wang F ( Institute of Pharmacology & Toxicology and Biochemical Pharmaceutics, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou, People's Republic of China)
Abstract	Human growth hormone (hGH) can mobilize lipid and inhibit the synthesis of triglycerides. However, it is not a potentially useful drug for treating obesity because it has many other actions resulting in several side effects. Here, we report a novel approach to develop the lipolytic function of hGH. The amino terminus of hGH was replaced by an inactive protein so that the actions unrelated to lipolytic function would be avoided. The fusion genes encoding human serum albumin (HSA) and lipolytic domain of hGH were constructed and expressed in Pichia pastoris. The recombinant proteins were purified and characterized by SDS-PAGE and Western blot. The preliminary stability tests demonstrated that HSA-hGH166-191 and HSA-hGH177-191 were stable at different pH levels after four days at 37°C. Lipolytic activity assay revealed that fusion proteins could increase the amounts of glycerol released from the isolated adipocytes. The HSA fusion proteins constructed in this work can be further developed as antiobesity agents.
File Format	HTM / HTML
ISSN	08854513
Issue Number	4
Volume Number	60
e-ISSN	14708744
Journal	Biotechnology and Applied Biochemistry
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2013-07-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Discipline Biotechnology Human Growth Hormone Chemistry Pharmacology Lipolysis Drug Effects Pichia Genetics Recombinant Fusion Proteins Isolation & Purification Serum Albumin Adipocytes Metabolism Animals Gene Expression Humans Male Protein Engineering Protein Stability Protein Structure, Tertiary Rats Rats, Wistar Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Drug Discovery Molecular Medicine Bioengineering Biomedical Engineering Applied Microbiology and Biotechnology Biotechnology Process Chemistry and Technology

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Expression, purification, and lipolytic activity of recombinant human serum albumin fusion proteins with one domain of human growth hormone in Pichia pastoris.

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