Solubilisation of myosin in a solution of low ionic strength l-histidine: Significance of the imidazole ring. (1st April 2016)
- Record Type:
- Journal Article
- Title:
- Solubilisation of myosin in a solution of low ionic strength l-histidine: Significance of the imidazole ring. (1st April 2016)
- Main Title:
- Solubilisation of myosin in a solution of low ionic strength l-histidine: Significance of the imidazole ring
- Authors:
- Chen, Xing
Zou, Yufeng
Han, Minyi
Pan, Lihua
Xing, Tong
Xu, Xinglian
Zhou, Guanghong - Abstract:
- Highlights: l -Histidine (His), imidazole (Imi) andl -carnosine (Car) increased solubility of myosin in low ionic strength solution. His, Imi and Car gave myosin suspensions with small particle size species. His, Imi and Car increased the absolute zeta potential of myosin suspension. His, Imi and Car induced conformational changes of soluble myosin. Imidazole ring was the significant constituent in His for solubilising myosin. Abstract: Myosin, a major muscle protein, can be solubilised in a low ionic strength solution containingl -histidine (His). To elucidate which chemical constituents in His are responsible for this solubilisation, we investigated the effects of 5 mM His, imidazole (Imi), l -α-alanine (Ala), 1-methyl-l -histidine (M-his) andl -carnosine (Car) on particle properties of myosin suspensions and conformational characteristics of soluble myosin at low ionic strength (1 mM KCl, pH 7.5). His, Imi and Car, each containing an imidazole ring, were able to induce a myosin suspension, which had small particle size species and high absolute zeta potential, thus increasing the solubility of myosin. His, Imi and Car affected the tertiary structure and decreased the α-helix content of soluble myosin. Therefore, the imidazole ring of His appeared to be the significant chemical constituent in solubilising myosin at low ionic strength solution, presumably by affecting its secondary structure.
- Is Part Of:
- Food chemistry. Volume 196(2016)
- Journal:
- Food chemistry
- Issue:
- Volume 196(2016)
- Issue Display:
- Volume 196, Issue 2016 (2016)
- Year:
- 2016
- Volume:
- 196
- Issue:
- 2016
- Issue Sort Value:
- 2016-0196-2016-0000
- Page Start:
- 42
- Page End:
- 49
- Publication Date:
- 2016-04-01
- Subjects:
- l-Histidine (PubChem CID: 6274) -- Imidazole (PubChem CID: 795) -- l-α-Alanine (PubChem CID: 5950) -- 1-Methyl-l-histidine (PubChem CID: 92105) -- l-Carnosine (PubChem CID: 439224)
Myosin -- l-Histidine -- Imidazole ring -- Solubility -- Chemical constituent
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2015.09.039 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2616.xml