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Complete Amino Acid Sequence and Structure Characterization of the Taste-modifying Protein, Miraculin

Theerasilp, S ; Hitotsuya, H ; Nakajo, S ; Nakaya, K ; Nakamura, Y ; Kurihara, Y

The Journal of biological chemistry, 1989-04, Vol.264 (12), p.6655-6659 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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Título:
Complete Amino Acid Sequence and Structure Characterization of the Taste-modifying Protein, Miraculin
Autor: Theerasilp, S ; Hitotsuya, H ; Nakajo, S ; Nakaya, K ; Nakamura, Y ; Kurihara, Y
Assuntos: Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Carboxypeptidases - metabolism ; Carboxypeptidases A ; Chromatography, High Pressure Liquid ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Glycoproteins - ultrastructure ; Molecular Sequence Data ; Molecular Weight ; Peptide Fragments - analysis ; Plant Proteins - ultrastructure ; Proteins ; Solubility
É parte de: The Journal of biological chemistry, 1989-04, Vol.264 (12), p.6655-6659
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: The taste-modifying protein, miraculin, has the unusual property of modifying sour taste into sweet taste. The complete amino acid sequence of miraculin purified from miracle fruits by a newly developed method (Theerasilp, S., and Kurihara, Y. (1988) J. Biol. Chem. 263, 11536–11539) was determined by an automatic Edman degradation method. Miraculin was a single polypeptide with 191 amino acid residues. The calculated molecular weight based on the amino acid sequence and the carbohydrate content (13.9%) was 24,600. Asn-42 and Asn-186 were linked N-glycosidically to carbohydrate chains. High homology was found between the amino acid sequences of miraculin and soybean trypsin inhibitor.
Editor: Bethesda, MD: Elsevier Inc
Idioma: Inglês

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Complete Amino Acid Sequence and Structure Characterization of the Taste-modifying Protein, Miraculin

Theerasilp, S ; Hitotsuya, H ; Nakajo, S ; Nakaya, K ; Nakamura, Y ; Kurihara, Y

Bethesda, MD: Elsevier Inc

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