Proteome changes on water-holding capacity of yak longissimus lumborum during postmortem aging

Proteome changes on water-holding capacity of yak longissimus lumborum during postmortem aging To study differentially expressed proteins on water-holding capacity (WHC) during postmortem aging of longissimus lumborum muscle, samples were classified according to drip loss into high and low drip loss groups. Fifty-five proteins were differentially abundant at days 0, 1 and 7 during postmortem aging and identified by MALDI TOF/TOF. The identified proteins can be divided into four main categories: metabolic enzymes, cell structural proteins, stress related proteins and transport proteins. Myosin light chain, heat shock protein 27 and triosephosphate isomerase showed a major difference between the two groups and may have the potential to be biological markers for WHC prediction. Furthermore, bioinformatics analysis revealed that the identified proteins were related to carbon metabolism, glycolysis and biosynthesis of amino acids and pyruvate metabolism. The functions of the identified proteins contribute to a more detailed molecular view of the processes behind WHC and are a valuable resource for future investigations. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Meat Science Elsevier

Proteome changes on water-holding capacity of yak longissimus lumborum during postmortem aging

Loading next page...
 
/lp/elsevier/proteome-changes-on-water-holding-capacity-of-yak-longissimus-lumborum-fdALGF3S88
Publisher
Elsevier
Copyright
Copyright © 2016 Elsevier Ltd
ISSN
0309-1740
D.O.I.
10.1016/j.meatsci.2016.07.010
Publisher site
See Article on Publisher Site

Abstract

To study differentially expressed proteins on water-holding capacity (WHC) during postmortem aging of longissimus lumborum muscle, samples were classified according to drip loss into high and low drip loss groups. Fifty-five proteins were differentially abundant at days 0, 1 and 7 during postmortem aging and identified by MALDI TOF/TOF. The identified proteins can be divided into four main categories: metabolic enzymes, cell structural proteins, stress related proteins and transport proteins. Myosin light chain, heat shock protein 27 and triosephosphate isomerase showed a major difference between the two groups and may have the potential to be biological markers for WHC prediction. Furthermore, bioinformatics analysis revealed that the identified proteins were related to carbon metabolism, glycolysis and biosynthesis of amino acids and pyruvate metabolism. The functions of the identified proteins contribute to a more detailed molecular view of the processes behind WHC and are a valuable resource for future investigations.

Journal

Meat ScienceElsevier

Published: Nov 1, 2016

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off