Solid-Phase Synthesis of Single-Chain Monellin, a Sweet Protein
スポンサーリンク
概要
- 論文の詳細を見る
Single-chain monellin, a sweet protein, was synthesized by stepwise solid-phase synthesis. After deprotection, and purification with HPLC, single-chain monellin was obtained in a yield of 0.3% based on the starting resin.
- 社団法人日本農芸化学会の論文
- 1998-10-23
著者
-
Ota Masafumi
Central Research Laboratories Ajinomoto Co. Inc.
-
Ariyoshi Yasuo
Central Research Laboratories Ajinomoto Co. Inc.
-
Ariyoshi Yasuo
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)
- 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
- 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)
- 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
- 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
- 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.