Evaluation of Molecular Interactions in Myosin, Fibrinogen, and Myosin-Fibrinogen Gels

E. Allen Foegeding, William R. Dayton, C. Eugene Allen

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Myosin, fibrinogen, and myosin-fibrinogen gels formed by heating at a rate of 12 °C/h were disrupted with guanidine hydrochloride, urea, and 2-mercaptoethanol. The degree of disruption was quantitated by turbidity, and complexes that remained soluble were analyzed by gel filtration in 6 M guanidine hydrochloride and SDS-polyacrylamide gel electrophoresis. Myosin and fibrinogen together or individually formed gels at 70 °C that were more difficult to solubilize than gels formed at 50 °C. Myosin and fibrinogen gels formed at 70 °C were stabilized by both noncovalent and disulfide bonds. Noncovalent and disulfide bonds are formed in myosin-fibrinogen gels at 50 and 70 °C.

Original languageEnglish (US)
Pages (from-to)559-563
Number of pages5
JournalJournal of agricultural and food chemistry
Volume35
Issue number4
DOIs
StatePublished - Jul 1 1987

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