Denaturation and aggregation of myosin from two bovine muscle types

Journal of Agricultural and Food Chemistry

Volumn 49, Issue 2, 2001, Pages 906-912

  Vega Warner, Virginia ^a   Smith, Denise M ^a,b  

^a Michigan State University   (United States)

^b UNIVERSITY OF IDAHO   (United States)

Author keywords

Aggregation; Bovine; Denaturation; Fiber type; Myosin; Ultimate ph

Indexed keywords

ISOPROTEIN; MYOSIN; MYOSIN HEAVY CHAIN;

ANIMAL; ANIMAL TISSUE; ARTICLE; CATTLE; COMPARATIVE STUDY; COW; DIFFERENTIAL SCANNING CALORIMETRY; FAST MUSCLE FIBER; FEMALE; HEAT; HEATING; MUSCLE; NONHUMAN; PH; PHASE TRANSITION; PHOTOMETRY; PROTEIN AGGREGATION; PROTEIN DENATURATION; SKELETAL MUSCLE; TEMPERATURE; TURBIDITY;

ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CATTLE; FEMALE; HEAT; MUSCLE FIBERS, FAST-TWITCH; MUSCLE, SKELETAL; MYOSINS; NEPHELOMETRY AND TURBIDIMETRY; PROTEIN DENATURATION; PROTEIN ISOFORMS;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0035117374     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf000565e     Document Type: Article

References (3)

1. Foegeding, E. A.; Liu, M. N. Functional differences of myofibrillar proteins from fast and slow twitch muscles. J. Muscle Foods 1995, 6, 109-123.
2. Pearson, A. M.; Young, R. B. Muscle and Meat Biochemistry; Academic Press: San Diego, CA, 1989.
3. Xiong, Y. L. Myofibrillar protein from different muscle fiber types: implications of biochemical and functional properties in meat processing. Crit. Rev. Food Sci. Nutr. 1994, 34, 293-320.