PORE-SIZE CONTROLLED AND POLY(ϵ-LYSINE)-IMMOBILIZED CELLULOSE SPHERICAL PARTICLES FOR REMOVAL OF LIPOPOLYSACCHARIDES

Todokoro, Masami; Sakata, Masayo; Matama, Satoshi; Kunitake, Masashi; Ohkuma, Kunio; Hirayama, Chuichi

doi:10.1081/jlc-120008814

Cited by 5 publications

(1 citation statement)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Selective adsorption to the cationic polymer resin is applied for protein solutions, but both negatively charged LPS and proteins are strongly adsorbed to the matrix. Given that background, various adsorbents of aminated cellulose beads have been developed. , Their benefits are that they provide high removal efficiency of LPS and high recovery yield of the protein.…”

Section: Resultsmentioning

confidence: 99%

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

et al. 2019

Self Cite

View full text Add to dashboard Cite

The protein cluster comprising a bovine hemoglobin (Hb) wrapped covalently by human serum albumins (HSAs), Hb–HSA m cluster (m = 3.0 ± 0.2), is a promising artificial O2 carrier as a red blood cell substitute. Evaluating the safety and efficacy of the Hb–HSA m cluster solution in preclinical and clinical tests necessitates enlargement of the preparation scale and establishment of a simple purification system. This paper describes details of the ideal synthesis of the Hb–HSA m cluster and its O2 binding property. Results show that (i) N-succinimidyl 3-maleimidopropionate (SMP) is an appropriate cross-linker and (ii) anion-exchange chromatography (AEC) is effective for purification. Soluble SMP allows the combination of Hb with HSA in a high protein concentration. Results demonstrate that AEC enables us to separate the cluster and HSA by increasing the ionic strength of the medium. Individual cluster components (Hb–HSA4, Hb–HSA3, Hb–HSA2, and Hb–HSA) showed equal O2 affinity. Furthermore, we conducted chromogenic limulus amebocyte lysate assay of lipopolysaccharides in the protein cluster solution.

show abstract

Section: Resultsmentioning

confidence: 99%

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

et al. 2019

Self Cite

View full text Add to dashboard Cite

show abstract

Poly‐ε‐Lysine Modified Nanocarbon Film Electrodes for LPS Detection

et al. 2014

View full text Add to dashboard Cite

We developed an electrochemical system for detecting lipopolysaccharide (LPS) that uses an ultraflat nanocarbon film electrode modified with poly‐ε‐lysine with a high affinity to LPS. LPS was captured on the modified electrode, and then ferrocene labeled polymyxin B (FcPMB) was captured on the LPS adsorbed electrode via the LPS‐PMB affinity interaction. The adsorbed FcPMB provided an amplified response with Fe2+ ions, and the current response was dependent on the amount of captured LPS (LOD=2.0 ng/mL). This was due to the efficient accumulation of the obtained current for LPS and the very low noise made possible by the ultraflat surface.

show abstract

Lipopolysaccharide removal affinity matrices based on novel cationic amphiphilic peptides

Sepahi

Hadadian

Cohan

et al. 2020

Preparative Biochemistry & Biotechnology

View full text Add to dashboard Cite

PORE-SIZE CONTROLLED AND POLY(ϵ-LYSINE)-IMMOBILIZED CELLULOSE SPHERICAL PARTICLES FOR REMOVAL OF LIPOPOLYSACCHARIDES

Cited by 5 publications

References 13 publications

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

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

Poly‐ε‐Lysine Modified Nanocarbon Film Electrodes for LPS Detection

Lipopolysaccharide removal affinity matrices based on novel cationic amphiphilic peptides

Contact Info

Product

Resources

About