Chemical Modification of Amino Groups in Mucor miehei Aspartyl Proteinase, Porcine Pepsin, and Chymosin : II. Conformational Stability(Food & Nutrition)

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概要

• 論文の詳細を見る

• The effects of chemical modification of amino groups on the conformational stability of Mucor miehei proteinase (MMP), porcine pepsin, and chymosin, the latter two being from mammalian sources, were examined using kinetic and thermodynamic analyses. Modification-induced stability reduction of only MMP was observed as demonstrated by a higher rate of guanidine hydro-chloride-induced denaturation, lower activation energy, decreased enthalpy of denaturation, and a substantially reduced free energy of denaturation. Results from this study corroborate those of a companion investigation indicating that MMP was more susceptible to destabilization by charge alteration than aspartyl proteinases of mammalian origin.

• 社団法人日本農芸化学会の論文
• 1991-08-23

著者

• Yada R

  Univ. Guelph Ontario Can

• Yada Rickey

  Department Of Food Science Ontario Agricultural College University Of Guelph

• Billings Gail

  Department Of Food Science University Of Guelph

• Smith Jeff

  Department Of Food Science University Of Guelph

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• Isolation, Purification, and Characterization of the Oligomeric Seed Globulin from Amaranthus hypochondriacus(Biological Chemistry)
• Chemical Modification of Amino Groups in Mucor miehei Aspartyl Proteinase, Porcine Pepsin, and Chymosin : II. Conformational Stability(Food & Nutrition)
• Chemical Modification of Amino Groups in Mucor miehei Aspartyl Proteinase, Porcing Pepsin, and Chymosin : I. Structure and Function(Food & Nutrition)

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