Premium
Tritium labelling of Thaumatin I, a sweet‐tasting protein from Thaumatococcus daniellii benth, by reductive methylation
Author(s) -
van Der Wel H.,
Wiersma A.,
Brouwer J. N.
Publication year - 1978
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.2580140511
Subject(s) - chemistry , thaumatin , tritium , sodium borohydride , methylation , lysine , labelling , yield (engineering) , borohydride , specific activity , radiochemistry , biochemistry , amino acid , enzyme , dna , physics , materials science , nuclear physics , metallurgy , gene , catalysis
Thaumatin I has been labelled by reductive methylation of four of the ε‐amino groups of the lysine residues in the protein with tritiated sodium borohydride. Methylation with unlabelled sodium borohydride showed that up to seven amino groups can be methylated without loss of sweet‐ness intensity. The yield of the tritium‐labelled methylated Thaumatin I was 31% with a tritium incorporation of 4.7%. Its specific radioactivity was 12.8 Ci/mmol.