Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles

To explore the interactive molecules of squid ink polysaccharides (SIP) for further understanding the action mechanisms of SIP bio-function, this study prepared SIP binding proteins from mouse liver using superparamagnetic nanometer beads. Michaelis–Menten constant (K(m)) was detected from a Linewea...

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Autores principales: Lin, Zhen, Tan, Xiaohui, Li, Fangping, Zhang, Yu, Luo, Ping, Lin, Xuan, Liu, Huazhong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8694236/
https://www.ncbi.nlm.nih.gov/pubmed/35424304
http://dx.doi.org/10.1039/d0ra09222c
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author Lin, Zhen
Tan, Xiaohui
Li, Fangping
Zhang, Yu
Luo, Ping
Lin, Xuan
Liu, Huazhong
author_facet Lin, Zhen
Tan, Xiaohui
Li, Fangping
Zhang, Yu
Luo, Ping
Lin, Xuan
Liu, Huazhong
author_sort Lin, Zhen
collection PubMed
description To explore the interactive molecules of squid ink polysaccharides (SIP) for further understanding the action mechanisms of SIP bio-function, this study prepared SIP binding proteins from mouse liver using superparamagnetic nanometer beads. Michaelis–Menten constant (K(m)) was detected from a Lineweaver–Burk double reciprocal plot to assess effect of SIP on activity of aldehyde oxidase (AOX). Results showed that three proteins, AOX-3, regucalcin (RGN) and α1-antitrypsin (A1AT3) were separated from mouse liver by magnetic nanoparticles conjugated with SIP. Contents of AOX-3 were much more than RGN and A1AT3. SIP (0.5 mg mL(−1)) reduced K(m) value of aldehyde oxidase of mouse liver from 91.79 μmol L(−1) to 43.70 μmol L(−1).
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spelling pubmed-86942362022-04-13 Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles Lin, Zhen Tan, Xiaohui Li, Fangping Zhang, Yu Luo, Ping Lin, Xuan Liu, Huazhong RSC Adv Chemistry To explore the interactive molecules of squid ink polysaccharides (SIP) for further understanding the action mechanisms of SIP bio-function, this study prepared SIP binding proteins from mouse liver using superparamagnetic nanometer beads. Michaelis–Menten constant (K(m)) was detected from a Lineweaver–Burk double reciprocal plot to assess effect of SIP on activity of aldehyde oxidase (AOX). Results showed that three proteins, AOX-3, regucalcin (RGN) and α1-antitrypsin (A1AT3) were separated from mouse liver by magnetic nanoparticles conjugated with SIP. Contents of AOX-3 were much more than RGN and A1AT3. SIP (0.5 mg mL(−1)) reduced K(m) value of aldehyde oxidase of mouse liver from 91.79 μmol L(−1) to 43.70 μmol L(−1). The Royal Society of Chemistry 2021-01-18 /pmc/articles/PMC8694236/ /pubmed/35424304 http://dx.doi.org/10.1039/d0ra09222c Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Lin, Zhen
Tan, Xiaohui
Li, Fangping
Zhang, Yu
Luo, Ping
Lin, Xuan
Liu, Huazhong
Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles
title Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles
title_full Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles
title_fullStr Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles
title_full_unstemmed Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles
title_short Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles
title_sort identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8694236/
https://www.ncbi.nlm.nih.gov/pubmed/35424304
http://dx.doi.org/10.1039/d0ra09222c
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