Change in Titin Position in Postmortem Bovine Muscle
T.P. Ringkob, B.B. Marsh, Marion L. Greaser
Abstract
T.P. Ringkob, B.B. Marsh, Marion L. Greaser
Abstract
ABSTRACT Myofibrils were prepared from bovine psoas muscles removed from the carcass at 3 and 48 hr postmortem and subsequently stained with a monoclonal antibody against titin. The antibody stained 2 bands per sarcomere (perpendicular to the fiber direction) in myofibrils from 3‐hr muscle but often revealed 4 bands per sarcomere in the 48‐hr samples. The results suggested that (1) the titin shape might be altered within the first 2 days postmortem, or (2) proteolysis of titin or a protein to which it was attached occurred.
OpenAlex reports 16 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
ABSTRACT Myofibrils were prepared from bovine psoas muscles removed from the carcass at 3 and 48 hr postmortem and subsequently stained with a monoclonal antibody against titin. The antibody stained 2 bands per sarcomere (perpendicular to the fiber direction) in myofibrils from 3‐hr muscle but often revealed 4 bands per sarcomere in the 48‐hr samples. The results suggested that (1) the titin shape might be altered within the first 2 days postmortem, or (2) proteolysis of titin or a protein to which it was attached occurred.
Key concepts: Titin, Sarcomere, Myofibril, Anatomy, Chemistry, Nebulin, Myosin, Rigor mortis