Inhibition of Angiotensin-Converting Enzyme by Synthetic Peptide Fragments of Various β-Caseins(Biological Chemistry)

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概要

• 論文の詳細を見る
• 社団法人日本農芸化学会の論文
• 1990-04-23

著者

• Nio Noriki

  Central Research Laboratories, Ajinomoto Co., Inc.

• Ariyoshi Yasuo

  Central Research Laboratories, Ajinomoto Co., Inc.

• Nio N

  Ajinomoto Co. Inc. Kanagawa Jpn

• Ariyoshi Y

  Ajinomoto Co. Inc. Kawasaki Jpn

• Ariyoshi Yasuo

  Central Research Laboratories Ajinomoto Co. Inc

• Kohmura M

  Ajinomoto Co. Inc. Kawasaki Jpn

• Kohmura Masanori

  Central Research Laboratories, Ajinomoto Co., Inc.

• Kohmura Masanori

  Central Research Laboratories Ajinomoto Co. Inc.

関連論文

• Enzymatic Synthesis and Chemical Properties of Sweet Aminomalonyl (Ama) Dipeptide Esters (R)-Ama-(S)-Phe-OMe and (R)-Ama-(S)-Phe-OEt
• N-Terminal Extension of Sweet Peptides in Relation to the Structural Features of Peptide Sweeteners(Organic Chemistry)
• Immobilization of Enzyme in Protein Films Prepared Using Transglutaminase(Food & Nutrition)
• α_-Casein Film Prepared Using Transglutaminase(Food & Nutrition)
• Solid-phase Synthesis and Structure-Taste Relationships of Analogs of the Sweet Protein Monellin
• Highly Probable Active Site of the Sweet Protein Monellin
• Solid-Phase Synthesis of [Asn^]-, [Asn^]-, [Gln^]-, and [Asn^]Monellin, Analogues of the Sweet Protein Monellin
• Solid-Phase Synthesis of Crystalline [Ser^] B-Chain Monellin, an Analogue of the Sweet Protein Monellin(Organic Chemistry)
• Solid-Phase Synthesis of Crystalline Monellin, a Sweet Protein(Organic Chemistry)
• Solid-Phase Synthesis and Crystallization of [Asn^, Gln^, Asn^]-A-Chain-[Asn^, Glu^]-B-Chain-Monellin, an Analogue of the Sweet Protein Monellin(Organic Chemistry)
• Complete Amino Acid Sequence of the Sweet Protein Monellin(Biological Chemistry)
• Solid-Phase Synthesis and Crystallization of Monellin, an Intensely Sweet Protein(Organic Chemistry)
• Inhibition of Angiotensin-Converting Enzyme by Synthetic Peptide Fragments of Various β-Caseins(Biological Chemistry)
• Inhibition of Angiotensin-Converting Enzyme by Synthetic Peptide Fragments of Human κ-Casein(Biological Chemistry)
• Inhibition of Angiotensin-converting Enzyme by Synthetic Peptides of Human β-Casein(Biological Chemistry)
• Location of the Disulfide Bonds of the Sweetness-suppressing Polypeptide Gurmarin
• Functional Properties of Heterologous Polymer Prepared by Transglutaminase between Milk Casein and Soybean Globulin(Food & Nutrition)
• Glutamine-specific Deamidation of α_-Casein by Transglutaminase(Food & Nutrition)
• Gelation of Protein Emulsion by Transglutaminase(Food & Nutrition)
• Inhibition of Prolyl Endopeptidase by Synthetic β-Casein Peptides and Their Derivatives with a C-Terminal Prolinol or Prolinal
• Inhibition of Prolyl Endopeptidase by Synthetic Peptide Fragments of Human β-Casein(Food & Nutrition)
• Functional Properties of Food Proteins Polymerized by Transglutaminase
• Synthesis, Folding, and Biological Activities of Peptide Fragments of Sweet Protein Monellin and Human Cystatin B (Stefin B)
• Solid-Phase Synthesis of Single-Chain Monellin, a Sweet Protein
• Total Synthesis of The Sweet Protein Mabinlin II
• Gelation Mechanism of Protein Solution by Transglutaminase
• The Synthesis of a Sweet Peptide, α-L-Aspartyl-L-phenylalanine Methyl Ester, without the Use of Protecting Groups
• A new synthesis of glutathione via the thiazoline peptide.
• The Reaction of Aspartyl Dipeptide Esters with Ketones
• Studies of Hydroxy Amino Acids. II. The Separation of Diastereoisomers of Hydroxy Amino Acids
• Gelation of Casein and Soybean Globulins by Transglutaminase
• The Convenient Preparation of L-Aspartic Anhydride Hydrochloride and Hydrobromide
• Studies of Hydroxy Amino Acids. I. Separation of Diastereoisomers of Threonine
• Structure-taste relationships of aspartyl tripeptide esters.
• Synthesis of aspartyl pentapeptide esters in relation to structural features of sweet peptides.
• The Structure-Taste Relationships of the Dipeptide Esters Composed of L-Aspartic Acid and β-Hydroxy Amino Acids
• Structure-taste relationships of aspartyl tetrapeptide esters.

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