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Preservation stability and in vivo administration of albumin–heme hybrid solution as an entirely synthetic O 2 ‐carrier
Author(s) -
Tsuchida Eishun,
Komatsu Teruyuki,
Yanagimoto Tetsuya,
Sakai Hiromi
Publication year - 2002
Publication title -
polymers for advanced technologies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.61
H-Index - 90
eISSN - 1099-1581
pISSN - 1042-7147
DOI - 10.1002/pat.240
Subject(s) - in vivo , albumin , human serum albumin , recombinant dna , heme , chemistry , in vitro , serum albumin , covalent bond , pharmacology , biochemistry , nuclear chemistry , biology , organic chemistry , enzyme , gene , microbiology and biotechnology
The recombinant human serum albumin incorporating a tetraphenylporphyrinatoiron(II) derivative with a covalently linked proximal base (rHSA‐FeP) is an entirely synthetic O 2 ‐carrier as a red blood cell substitute. It shows long‐term preservation stability of both solution properties and O 2 ‐binding ability over a broad temperature range including room temperature. The physicochemical parameters of the rHSA‐Fe(II)P solution ([rHSA]: 5 wt%) stored at 5–40 °C have remained constant over one year. The in vivo safety of this material was also studied by the survival tests and clinical blood chemistry assays. All rats given the 5 wt% rHSA‐Fe(II)P solution have been alive for 14 days after the infusion. During the observation period, no remarkable reaction was seen in the appearance of the animals. Parameters of the clinical blood serum chemistry were all in the normal ranges, and pathological inspections of the major organs showed no significant infarct in their tissues. Copyright © 2003 John Wiley & Sons, Ltd.