Physiological action and structure characteristics of the sweet-tasting proteins thaumatin and monellin
- 31 May 1980
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 5 (5) , 122-123
- https://doi.org/10.1016/0968-0004(80)90052-3
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
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- Conformational transitions of monellin, an intensely sweet proteinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein MonellinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- Spectrometric Investigation of Thaumatin I and II, Two Sweet‐Tasting Proteins from Thaumatococcus daniellii BenthEuropean Journal of Biochemistry, 1973
- Isolation and Characterization of Thaumatin I and II, the Sweet‐Tasting Proteins from Thaumatococcus daniellii BenthEuropean Journal of Biochemistry, 1972
- Isolation and characterization of the sweet principle fromDioscoreophyllum cumminsii (stapf) DielsFEBS Letters, 1972
- Purification of monellin, the sweet principle of Dioscoreophyllum cumminsiiBiochimica et Biophysica Acta (BBA) - General Subjects, 1972