1988Journal of Food ScienceRequires access

Change in Titin Position in Postmortem Bovine Muscle

T.P. Ringkob, B.B. Marsh, Marion L. Greaser

Open publisher page 16 citations

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.

About this research paper

What this paper is about

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.

Why it matters

OpenAlex reports 16 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available 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.

Key concepts: Titin, Sarcomere, Myofibril, Anatomy, Chemistry, Nebulin, Myosin, Rigor mortis

Related papers

Back to paper searchBrowse research topicsOriginal source
Change in Titin Position in Postmortem Bovine Muscle — Research Paper | ScholarLens