Gel Electrophoretic Analysis of the Protein Changes in Ground Beef Stored at 2°C

Y. L. XIONG, A. F. ANGLEMIER

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

Purified myofibrils and sarcoplasmic proteins were prepared from ground (GR) and intact (CON) beef semitendinosus muscle samples after 0, 1, 3, 6, and 10 days of storage at 2°C. SDS‐polyacrylamide gel electrophoresis analysis revealed the following major postmortem changes in GR samples: the gradual disappearance of nebulin and desmin, appearance of 110,000‐, 95,000‐ and 30,000‐dalton polypeptides, and an increased content of myosin light chain‐3 and 55,000‐dalton component in myofibrils. Also noted was emergence of 100,000‐ and −500,000‐dalton polypeptides and diminution of 300,000‐dalton protein in the sarcoplasmic fraction. Since GR samples showed proteolytic changes similar to those of CON samples, it was concluded that grinding had little effect on postmortem muscle protein degradation.

Original languageEnglish
Pages (from-to)287-290
Number of pages4
JournalJournal of Food Science
Volume54
Issue number2
DOIs
StatePublished - Mar 1989

ASJC Scopus subject areas

  • Food Science

Fingerprint

Dive into the research topics of 'Gel Electrophoretic Analysis of the Protein Changes in Ground Beef Stored at 2°C'. Together they form a unique fingerprint.

Cite this