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In vitro degradation of bovine myofi...

Mohrhauser, Dustin Andrew.

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In vitro degradation of bovine myofibrils is caused by mu-calpain, not caspase-3.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	In vitro degradation of bovine myofibrils is caused by mu-calpain, not caspase-3./
Author:	Mohrhauser, Dustin Andrew.
Description:	80 p.
Notes:	Source: Masters Abstracts International, Volume: 49-01, page: 0230.
Contained By:	Masters Abstracts International49-01.
Subject:	Agriculture, Food Science and Technology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1485833
ISBN:	9781124199474

In vitro degradation of bovine myofibrils is caused by mu-calpain, not caspase-3.
Mohrhauser, Dustin Andrew.

In vitro degradation of bovine myofibrils is caused by mu-calpain, not caspase-3. - 80 p.

Source: Masters Abstracts International, Volume: 49-01, page: 0230.

Thesis (M.S.)--South Dakota State University, 2010.

Tenderness is a key palatability trait influencing consumers' perception of meat quality and is influenced by a multitude of factors, including postmortem proteolysis. A fundamental understanding of this biological mechanism regulating tenderness is necessary to decrease variability and increase consumer satisfaction. However, reports regarding the enzyme systems involved in postmortem tenderization are conflicting. Therefore, the objective of this study was to determine if caspase-3 is responsible for the degradation of myofibrillar proteins during aging. Analysis of western blots revealed no change in abundance of intact troponin-T, desmin, titin, or nebulin over time in myofibrils incubated with caspase-3. However, abundance of these proteins subjected to digestion with mu-calpain and mu-calpain + caspase-3 revealed degradation patterns similar to in vivo samples. No degradation of alpha-actinin was observed in either in vitro or in vivo samples. Results of this study indicate mu-calpain, not caspase-3, is responsible for degradation of specific myofibrillar proteins during beef aging.

ISBN: 9781124199474Subjects--Topical Terms:

1017813
Agriculture, Food Science and Technology.

In vitro degradation of bovine myofibrils is caused by mu-calpain, not caspase-3.
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020 $a 9781124199474
035 $a (UMI)AAI1485833
035 $a AAI1485833
040 $a UMI $c UMI
100 1 $a Mohrhauser, Dustin Andrew. $3 1677109
245 1 0 $a In vitro degradation of bovine myofibrils is caused by mu-calpain, not caspase-3.
300 $a 80 p.
500 $a Source: Masters Abstracts International, Volume: 49-01, page: 0230.
500 $a Adviser: Amanda Weaver.
502 $a Thesis (M.S.)--South Dakota State University, 2010.
520 $a Tenderness is a key palatability trait influencing consumers' perception of meat quality and is influenced by a multitude of factors, including postmortem proteolysis. A fundamental understanding of this biological mechanism regulating tenderness is necessary to decrease variability and increase consumer satisfaction. However, reports regarding the enzyme systems involved in postmortem tenderization are conflicting. Therefore, the objective of this study was to determine if caspase-3 is responsible for the degradation of myofibrillar proteins during aging. Analysis of western blots revealed no change in abundance of intact troponin-T, desmin, titin, or nebulin over time in myofibrils incubated with caspase-3. However, abundance of these proteins subjected to digestion with mu-calpain and mu-calpain + caspase-3 revealed degradation patterns similar to in vivo samples. No degradation of alpha-actinin was observed in either in vitro or in vivo samples. Results of this study indicate mu-calpain, not caspase-3, is responsible for degradation of specific myofibrillar proteins during beef aging.
590 $a School code: 0205.
650 4 $a Agriculture, Food Science and Technology. $3 1017813
650 4 $a Agriculture, Animal Culture and Nutrition. $3 1017857
690 $a 0359
690 $a 0475
710 2 $a South Dakota State University. $3 1019395
773 0 $t Masters Abstracts International $g 49-01.
790 1 0 $a Weaver, Amanda, $e advisor
790 $a 0205
791 $a M.S.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1485833