Isolation and characterisation of tropomyosin from shrimp (Penaeus vannamei Boone) and its association property at high ionic strength

Natural Product Research

Volumn 30, Issue 1, 2016, Pages 115-119

  Huang, Luyao ^a,b   Du, Bingjian ^a   Bai, Guangling ^a   Wang, Qunqun ^a   Zhao, Guanghua ^a,c   Ning, Yong ^c  

^a CHINA AGRICULTURAL UNIVERSITY   (China)

^b Sichuan Institute for Food and Drug Control   (China)

^c HUBEI UNIVERSITY OF CHINESE MEDICINE   (China)

Author keywords

nanofibres; purification; self assembly; shrimp; tropomyosin

Indexed keywords

TROPOMYOSIN; ADENOSINE TRIPHOSPHATE; ALLERGEN; NANOFIBER;

ARTICLE; IONIC STRENGTH; LITOPENAEUS VANNAMEI; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN ISOLATION; PROTEIN POLYMERIZATION; PROTEIN PURIFICATION; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; FOOD ALLERGY; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; METABOLISM; MOLECULAR WEIGHT; OSMOLARITY; PENAEIDAE;

ADENOSINE TRIPHOSPHATE; ALLERGENS; AMINO ACID SEQUENCE; ANIMALS; CHROMATOGRAPHY, ION EXCHANGE; FOOD HYPERSENSITIVITY; MOLECULAR WEIGHT; NANOFIBERS; OSMOLAR CONCENTRATION; PENAEIDAE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TROPOMYOSIN;

EID: 84962635148     PISSN: 14786419     EISSN: 14786427     Source Type: Journal    
DOI: 10.1080/14786419.2015.1033622     Document Type: Article

References (13)

1. C.Akkermans, P.Venema, A.J.van der Goot, H.Gruppen, E.J.Bakx, R.M.Boom, E.van der Linden. 2008. Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2. Biomacromolecules. 9:1474–1479. doi:10.1021/bm7014224.
2. M.Albrecht, S.Alessandri, A.Conti, A.Reuter, I.Lauer, S.Vieths, G.Reese. 2008. High level expression, purification and physico – and immunochemical characterisation of recombinant Pen a 1: a major allergen of shrimp. Mol Nutr Food Res. 52:S186–S195.
3. W.Astbury, R.Reed, L.Spark. 1948. An X-ray and electron microscope study of tropomyosin. Biochem J. 43:282.
4. D.M.Helfman, S.Cheley, E.Kuismanen, L.A.Finn, Y.Yamawaki-Kataoka. 1986. Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation. Mol Cell Biol. 6:3582–3595.
5. G.M.Liu, H.Cheng, J.B.Nesbit, W.J.Su, M.J.Cao, S.J.Maleki. 2010. Effects of boiling on the IgE-binding properties of tropomyosin of shrimp (Litopenaeus vannamei). J Food Sci. 75:T1–T5. doi:10.1111/j.1750-3841.2009.01391.x.
6. A.L.Lopata, S.B.Lehrer. 2009. New insights into seafood allergy. Curr Opin Allergy Clin Immunol. 9:270–277. doi:10.1097/ACI.0b013e32832b3e6f.
7. S.M.Loveday, J.Su, M.A.Rao, S.G.Anema, H.Singh. 2011. Effect of calcium on the morphology and functionality of whey protein nanofibrils. Biomacromolecules. 12:3780–3788. doi:10.1021/bm201013b.
8. V.S.Rao, E.N.Marongelli, W.H.Guilford. 2009. Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit. Cell Motil Cytoskeleton. 66:10–23. doi:10.1002/cm.20321.
9. J.Sodek, R.Hodges, L.Smillie, L.Jurasek. 1972. Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. P Natl Acad Sci. 69:3800–3804. doi:10.1073/pnas.69.12.3800.
10. A.D.Sousa, C.S.Farah. 2002. Quantitative analysis of tropomyosin linear polymerization equilibrium as a function of ionic strength. J Biol Chem. 277:2081–2088. doi:10.1074/jbc.M109568200.
11. D.Sousa, A.Cammarato, K.Jang, P.Graceffa, L.S.Tobacman, X.E.Li, W.Lehman. 2010. Electron microscopy and persistence length analysis of semi-rigid smooth muscle tropomyosin strands. Biophys J. 99:862–868. doi:10.1016/j.bpj.2010.05.004.
12. W.F.Stafford, E.Lee, P.Graceffa. 2012. Equilibrium self-association of tropomyosin. FEBS Lett. 586:3840–3842. doi:10.1016/j.febslet.2012.08.035.
13. A.Wegner. 1979. Equilibrium of the actin-tropomyosin interaction. J Mol Biol. 131:839–853. doi:10.1016/0022-2836(79)90204-3.