Premium
SDS‐PAGE Conditions for Detection of Titin and Nebulin in Tender and Tough Bovine Muscles
Author(s) -
PATERSON B. C.,
PARRISH F. C.
Publication year - 1987
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1987.tb06659.x
Subject(s) - nebulin , myofibril , titin , chemistry , acrylamide , sodium dodecyl sulfate , gel electrophoresis , chromatography , biochemistry , sarcomere , biology , myocyte , monomer , microbiology and biotechnology , organic chemistry , polymer
Purified myofibrils were prepared from infraspinatus (tender) and rhomboideus (tough) muscles at 7 days postmortem and examined for myofibrillar/cytoskeleta1 protein degradation by using sodium dodecyl sulfate polyactylamide gel electrophoresis (SDS‐PAGE). Four acrylamide/bisacrylamide ratios (37:1, 50:1, 75:l and 100:1) and two SDS‐PAGE gel buffers (Tris‐HCl, pH 8.0 and 8.9) were used to determine the optimum conditions for detection of titin and nebulin. Titin was degraded to a greater extent in myofibrils from the infraspinatus than in myofibrils from the rhomboideus . Very little nebulin was detected in either muscle. Use of acrylamide/bisacrylamide ratio of 37:1 and a gel buffer of pH 8.0 provided the most optimum conditions for detecting differences in the resolution of titin, nebulin and their apparent degradation products.