FUNCTIONAL DIFFERENCES OF MYOFIBRILLAR PROTEINS FROM FAST AND SLOW TWITCH MUSCLES
Author:
Publisher
Wiley
Subject
Food Science
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1745-4573.1995.tb00561.x/fullpdf
Reference49 articles.
1. Endurance-exercised growing sheep: I. Post-mortem and histological changes in skeletal muscles
2. Endurance-exercised growing sheep: II. Tenderness increase and change in meat quality
3. Influence of Poultry Species, Muscle Groups, and NaCl Level on Strength, Deformability, and Water Retention in Heat-Set Muscle Gels
4. Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress.
5. Functionality of muscle proteins in gelation mechanisms of structured meat products
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1. Dependence of microbial transglutaminase on meat type in myofibrillar proteins cross-linking;Food Chemistry;2009-01
2. Thermal gelation of brown trout myofibrils from white and red muscles: effect of pH and ionic strength;Journal of the Science of Food and Agriculture;2002
3. Denaturation and Aggregation of Myosin from Two Bovine Muscle Types;Journal of Agricultural and Food Chemistry;2001-01-05
4. Composition, solubility and gel properties of salt soluble proteins from two bovine muscle types;Meat Science;1999-03
5. Determination of Surface Hydrophobicity of Fast and Slow Myosins from Rabbit Skeletal Muscles: Implication in Heat-Induced Gelation;Journal of the Science of Food and Agriculture;1996-11
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