Protein–surfactant interactions between bovine lactoferrin and [PDF]

Jan 19, 2017 - Full Text · PDF (2617 K) · PDF-Plus (557 K); Citing articles. Protein–surfactant interactions between bovine lactoferrin and sophorolipids under neutral and acidic conditions. Kentaro Matsumiya, Yasushi A. Suzuki, Yoshihiko Hirata, Yuko Nambu, Yasuki Matsumura. aLaboratory of Quality Analysis and ...

3 downloads 26 Views 382KB Size

Recommend Stories


bovine lactoferrin
You miss 100% of the shots you don’t take. Wayne Gretzky

Bovine lactoferrin for Helicobacter pylori eradication
Keep your face always toward the sunshine - and shadows will fall behind you. Walt Whitman

Bovine Lactoferrin Activity Against Chikungunya and Zika Viruses
Every block of stone has a statue inside it and it is the task of the sculptor to discover it. Mich

Interactions Between Saliency and Utility
Learning never exhausts the mind. Leonardo da Vinci

Lactoferrin
If you want to go quickly, go alone. If you want to go far, go together. African proverb

Lactoferrin
Happiness doesn't result from what we get, but from what we give. Ben Carson

Interactions between Phospholipid Monolayers
If your life's work can be accomplished in your lifetime, you're not thinking big enough. Wes Jacks

Interactions between somite cells
If you want to go quickly, go alone. If you want to go far, go together. African proverb

Thermally driven interactions between
Open your mouth only if what you are going to say is more beautiful than the silience. BUDDHA

Idea Transcript


Login

Register

Shibboleth

Mobile

Cart

Advanced Search

A division of Canadian Science Publishing a not-for-profit publisher

All Journals

Search

Biochemistry and Cell Biology Home

CSP

Journals

Books

Compilations

Open Access

Authors

Librarians

Societies

About the Press

Contact

Français

Home > Journals > Biochemistry and Cell Biology > List of Issues > Volume 95, Number 1, February 2017 > Protein–surfactant interactions between bovine lactoferrin and sophoro...

Article

« Previous TOC Next »

Protein–surfactant interactions between bovine lactoferrin and sophorolipids under neutral and acidic conditions1

Full Text PDF (2617 K) PDF-Plus (561 K) Citing articles

Kentaro Matsumiya,a Yasushi A. Suzuki,b Yoshihiko Hirata,b Yuko

Browse the journal List of issues e-First articles

a Laboratory of Quality Analysis and Assessment, Division of Agronomy and Horticultural Science,

Email a Colleague

Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.

Reprints & Permissions

b Lactoferrin Laboratory, Saraya Co., Ltd., 2-2-8 Yuzato, Higashisumiyoshi-ku, Osaka 546-0013, Japan.

Citation Alerts

Corresponding author: Kentaro Matsumiya (email: [email protected]).

Download Adobe Reader for PDFs

Current issue

Copyright remains with the author(s) or their institution(s). Permission for reuse (free in most cases) can be obtained from RightsLink.

Most cited articles

For authors About the journal Open Access Benefits and services Instructions to authors

2

Journal Tools Instructions to authors

Published on the web 19 January 2017. Received March 30, 2016. Accepted October 16, 2016.

Get an email alert for the latest issue

Biochemistry and Cell Biology, 2017, 95(1): 126-132, https://doi.org/10.1139/bcb-2016-0057

Check out the journal's featured content

Sample issue Author index

Share

Add to Favorites Download Citation

1 This Article is part of a Special Issue from the XIIth Lactoferrin Conference.

Most read articles

Tweet

Like 0

Nambu,a Yasuki Matsumura a

Just-IN articles

Special issues

Article Tools



ABSTRACT To understand the protein–surfactant interactions between naturally derived sophorolipids (SLs) and bovine lactoferrin (bLf), we carried out spectroscopic, microscopic, and biochemical experiments under weakly acidic and neutral pH conditions. Particle size analysis, microscopy, and enzymatic digestion indicated that bLf and SLs interact with each other to form sheet-like and small aggregated structures reflecting the original self-organization of SLs at pH 5.0 and 7.0, respectively. Circular dichroism (CD) showed that SLs did not significantly affect the secondary structure of bLf.



Follow the Journal

Subscribe Now or click here for more information

Keywords: lactoferrin, sophorolipids, protein–surfactant interaction, complex, electrostatic interaction

Submit a manuscript Permission forms

References

Reprints & permissions to reuse content

Alizadeh-Pasdar N, Li-Chan ECY. 2000. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. J. Agric. Food Chem. 48: 328-334 Crossref, Medline. Brines RD, Brock JH. 1983. The effect of trypsin and chymotrypsin on the in vitro antimicrobial and iron-binding properties of lactoferrin in human milk and bovine colostrum: unusual resistance of human apolactoferrin to proteolytic digestion. Biochim. Biophys. Acta, Gen. Subj. 759: 229-235 Crossref, Medline. De S, Girigoswami A, Das S. 2005. Fluorescence probing of albumin-surfactant interaction. J. Colloid Interface Sci. 285: 562-573 Crossref, Medline. Fasman, G.D. 1978. Circular dichroism analysis of chromatin and DNA–nuclear protein complexes. In Methods in cell biology. Vol. 18: Chromatin and chromosomal protein research III. Edited by G. Stein, J. Stein, and L.J. Kleinsmith. Academic Press, New York. pp. 327–349. 10.1016/S0091679X(08)60145-4. Crossref Groves ML. 1960. The isolation of a red protein from milk. J. Am. Chem. Soc. 82: 3345-3350 Crossref, ISI. Hawe A, Sutter M, Jiskoot W. 2008. Extrinsic fluorescent dyes as tools for protein characterization. Pharm. Res. 25: 1487-1499 Crossref, Medline. Hayakawa S, Nakai S. 1985. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J. Food Eng. 50: 486-491 Crossref. Haynes DH, Staerk H. 1974. 1-Anilino-8-naphthalenesulfonate: a fluorescent probe of membrane surface structure, composition and mobility. J. Membr. Biol. 17: 313-340 Crossref, Medline. Hu F, Pan F, Sawano Y, Makino T, Kakehi Y, Komiyama M, et al. 2008. Studies of the structure of multiferric ion-bound lactoferrin: a new antianemic edible material. Int. Dairy J. 18: 1051-1056 Crossref. Hu Y, Ju L. 2001. Purification of lactonic sophorolipids by crystallization. J. Biotechnol. 87: 263-272 Crossref, Medline. Imura T, Morita T, Fukuoka T, Ryu M, Igarashi K, Hirata Y, Kitamoto D. 2014. Spontaneous vesicle formation from sodium salt of acidic sophorolipid and its application as a skin penetration enhancer. J. Oleo Sci. 63: 141-147 Crossref, Medline. Ishii N, Kobayashi T, Matsumiya K, Ryu M, Hirata Y, Matsumura Y, Suzuki YA. 2012. Transdermal administration of lactoferrin with sophorolipid. Biochem. Cell Biol. 90: 504-512 Link. Abstract Kato A, Nakai S. 1980. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta, Protein Struct. 624: 13-20 Crossref, Medline. Konishi M, Fukuoka T, Morita T, Imura T, Kitamoto D. 2008. Production of new types of sophorolipids by Candida batistae. J. Oleo Sci. 57: 359-369 Crossref, Medline. Lang, S. 2003. Surfactants produced by microorganisms. In Novel surfactants: preparation applications and biodegradability. 2nd ed. Edited by K. Holmberg. CRC Press, New York. pp. 279– 316.

What we're blogging about

Lönnerdal, B., and Suzuki, Y.A. 2013. Lactoferrin. In Advanced dairy chemistry. Vol. 1A: Proteins: basic aspects. 4th ed. Edited by P.L.H. McSweeney and P.F. Fox. Springer, New York. pp. 295–315. 10.1007/978-1-4614-4714-6_10. Crossref

Angélina Lacroix: APNM Undergraduate Research Excellence Award Winner

Moore SA, Anderson BF, Groom CR, Haridas M, Baker EN. 1997. Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution. J. Mol. Biol. 274: 222-236 Crossref, Medline, ISI.

Posted: Dec 30, 2017 Canadian Science Publishing sponsors the Applied Physiology, Nutrition, and Metabolism Undergraduate Research Excellence Awards, which are awarded in partnership with…

Nuñez A, Ashby R, Foglia TA, Solaiman DKY. 2001. Analysis and characterization of sophorolipids by liquid chromatography with atmospheric pressure chemical ionization. Chromatographia 53: 673-677 Crossref. Shimazaki K, Kawaguchi A, Sato T, Ueda Y, Tomimura T, Shimamura S. 1993. Analysis of human and bovine milk lactoferrins by rotofor and chromatofocusing. Int. J. Biochem. 25: 1653-1658 Crossref, Medline.

The Experiences of Female Students in an Introductory Physics Course

Sørensen M, Sørensen SPL. 1940. The proteins in whey. C. R. Trav. Lab. Carlsberg, Ser. Chim. 23: 55-99 . Tang L, Wu JJ, Ma Q, Cui T, Andreopoulos FM, Gil J, et al. 2010. Human lactoferrin stimulates skin keratinocyte function and wound re-epithelialization. Br. J. Dermatol. 163(1): 38-47 Crossref, Medline.

Posted: Dec 28, 2017 By Emily Marshman, Zeynep Y. Kalender, Timothy Nokes-Malach, Christian Schunn, and Chandralekha Singh Imagine you are sitting in a classroom…

Van Bogaert, INA, Zhang J, Soetaert W. 2011. Microbial synthesis of sophorolipids. Process Biochem. 46: 821-833 Crossref. Zhou S, Xu C, Wang J, Gao W, Akhverdiyeva R, Shah V, Gross R. 2004. Supramolecular assemblies of a naturally derived sophorolipid. Langmuir 20(19): 7926-7932 Crossref, Medline.

Cited by View all 4 citing articles

Lactoferrin researchers descend on Nagoya Castle David B. Alexander, Hans J. Vogel, Hiroyuki Tsuda Biochemistry and Cell Biology, 2017, 95(1): 1-4, https://doi.org/10.1139/bcb2017-0009 Full Text

Connect With Us

Alerts

PDF (890 K)

CSP Blog

» Citation

PDF Plus (218 K)

Facebook

Twitter

YouTube

© Copyright 2018 – Canadian Science Publishing

Flickr

Linked In

RSS

Smile Life

When life gives you a hundred reasons to cry, show life that you have a thousand reasons to smile

Get in touch

© Copyright 2015 - 2024 PDFFOX.COM - All rights reserved.