HEAT‐INDUCED TRANSITIONS IN THE PROTEIN‐PROTEIN INTERACTION OF BOVINE NATURAL ACTOMYOSIN

Gregory Ray Ziegler, J. C. ACTON

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Protein‐protein interaction of bovine natural actomyosin (NAM) was studied by means of optical density changes resulting from discrete particle formation in the temperature range of4°C to 70°C. From Arrhenius plots, the apparent heat of activation (ΔHa) at pH 5.5 (17.1 kcallmole) was significantly (P<0.05) lower than activation energies in the pH range of 6.0 to 7.5. The lower Δ Ha resulted in initiation of protein‐protein interaction at a temperature near 16°C at pH 5.5, whereas interaction did not proceed until the temperature approached 37°C at pH 6.0 and above. Derivative curves (dOD/dT) at pH 5.5 and 6.0 showed two distinct NAM thermal transition regions. Tm1 occurred at 43.0°C at pH 5.5 and 48.5°C at pH 6.0, with the 5.5°C difference possibly arising from effects of proton binding in altering protein conformation. Only a 1.5°C difference in Tm2 (56.0°C at pH 5.5 versus 57.5°C at pH 6.0) was found. Although the overall heat‐mediated NAM aggregation (in dilute solution) was found to follow first order kinetics by two evaluation methods, the existence of two thermal transitions supports a two‐step reaction mechanism proposed for the formation of protein gels (in higher concentration solutions).

Original languageEnglish (US)
Pages (from-to)25-38
Number of pages14
JournalJournal of Food Biochemistry
Volume8
Issue number1
DOIs
StatePublished - Jan 1 1984

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Actomyosin
cattle
Hot Temperature
heat
Temperature
protein conformation
Protein Conformation
temperature
reaction mechanisms
activation energy
protons
absorbance
Protons
binding proteins
chemical derivatives
Gels
gels
kinetics

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Food Science
  • Pharmacology
  • Cell Biology

Cite this

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title = "HEAT‐INDUCED TRANSITIONS IN THE PROTEIN‐PROTEIN INTERACTION OF BOVINE NATURAL ACTOMYOSIN",
abstract = "Protein‐protein interaction of bovine natural actomyosin (NAM) was studied by means of optical density changes resulting from discrete particle formation in the temperature range of4°C to 70°C. From Arrhenius plots, the apparent heat of activation (ΔHa) at pH 5.5 (17.1 kcallmole) was significantly (P<0.05) lower than activation energies in the pH range of 6.0 to 7.5. The lower Δ Ha resulted in initiation of protein‐protein interaction at a temperature near 16°C at pH 5.5, whereas interaction did not proceed until the temperature approached 37°C at pH 6.0 and above. Derivative curves (dOD/dT) at pH 5.5 and 6.0 showed two distinct NAM thermal transition regions. Tm1 occurred at 43.0°C at pH 5.5 and 48.5°C at pH 6.0, with the 5.5°C difference possibly arising from effects of proton binding in altering protein conformation. Only a 1.5°C difference in Tm2 (56.0°C at pH 5.5 versus 57.5°C at pH 6.0) was found. Although the overall heat‐mediated NAM aggregation (in dilute solution) was found to follow first order kinetics by two evaluation methods, the existence of two thermal transitions supports a two‐step reaction mechanism proposed for the formation of protein gels (in higher concentration solutions).",
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HEAT‐INDUCED TRANSITIONS IN THE PROTEIN‐PROTEIN INTERACTION OF BOVINE NATURAL ACTOMYOSIN. / Ziegler, Gregory Ray; ACTON, J. C.

In: Journal of Food Biochemistry, Vol. 8, No. 1, 01.01.1984, p. 25-38.

Research output: Contribution to journalArticle

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