Hemoglobin–Albumin Clusters Prepared Using N-Succinimidyl 3-Maleimidopropionate as an Appropriate Cross-Linker-Reference-Cited by-同舟云学术

Hemoglobin–Albumin Clusters Prepared Using N-Succinimidyl 3-Maleimidopropionate as an Appropriate Cross-Linker

Published:2019-02-14 Issue:2 Volume:4 Page:3228-3233
ISSN:2470-1343
Container-title:ACS Omega
language:en
Short-container-title:ACS Omega

Author:

Funaki Ryosuke¹,Kashima Tomonori¹,Okamoto Wataru¹,Sakata Sho¹,Morita Yoshitsugu¹^ORCID,Sakata Masayo²,Komatsu Teruyuki¹^ORCID

Affiliation:

1. Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551, Japan

2. Department of Applied Chemistry and Biochemistry, Graduate School of Science and Technology, Kumamoto University, 2-39-1 Kurokami, Chuo-ku, Kumamoto-shi, Kumamoto 860-8555, Japan

Funder

Naito Foundation

Japan Society for the Promotion of Science

Institute of Science and Engineering, Chuo University

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acsomega.8b03474

Reference31 articles.

1. World Health Organization (WHO). Blood safety and availability, 22 June 2017. http://www.who.int/news-room/fact-sheets/detail/blood-safety-and-availability (accessed on Dec 12, 2018).

2. Comprehensive Biochemical and Biophysical Characterization of Hemoglobin-Based Oxygen Carrier Therapeutics: All HBOCs Are Not Created Equally

3. Isolation and characterization of a new hemoglobin derivative cross-linked between the alpha chains (lysine 99 alpha 1----lysine 99 alpha 2).

4. Site-Specific Cross-Linking of Human and Bovine Hemoglobins Differentially Alters Oxygen Binding and Redox Side Reactions Producing Rhombic Heme and Heme Degradation

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