Physicochemical Properties and Crystal Structures of Recombinant Canine and Feline Serum Albumins

DOI:10.15011//jasma.36.360104
Int. J. Microgravity Sci. Appl. 2019p360104
Author
T. KOMATSU, K. KIHIRA, K. YAMADA, K. YOKOMAKU, M. AKIYAMA and Y. MORITA
Organization
Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, JEM Utilization Center, Human Spaceflight Technology Directorate, Japan Aerospace Exploration Agency (JAXA)
Abstract
Serum albumin is the most prominent plasma protein in the blood circulatory system and is the main transporter of various compounds. Although ligand binding ability and crystal structure of human serum albumin (HSA) have been widely studied, there are only few reports on serum albumins of companion animals, particularly dogs and cats. This review describes the synthesis, physicochemical properties, and crystal structures of recombinant canine serum albumin (rCSA) and feline serum albumin (rFSA). The rCSA and rFSA were produced in a gram quantity by genetic engineering procedure using Pichia yeast. The proteins show identical features to those of the native CSA and FSA derived from canine and feline plasma. Single crystals of rFSA were prepared under a microgravity environment in the International Space Station. The overall structures of rCSA and rFSA closely resemble to that of HSA. These recombinant serum albumins are anticipated for use as a therapeutic reagent that can be exploited in numerous veterinary medicine situations.
Keyword(s)
Recombinant Protein, Crystal Structure Analysis, High-Quality Protein Crystal Growth Experiment, International Space Station, Veterinary Medicine.
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Received 27 September 2018, Accepted 20 November 2018, Published 31 January 2019

© The Japan Society of Microgravity Applicaiton

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