Interaction of allylisothiocyanate with bovine serum albumin.

The interaction of aiJYli~()thiocyanate with bovine serum albumin
was monitored by fluorescence titration. The interaction was weak with an apparent
asso.::iation constau[ of 2 x 1O~. The interaction was unaffected in the pH range
of 5·0 to 8·3 and by Nae!. However, the addition of dioxane upto 4% increased
the value of the assodation constant. N-Methyl bovine serum albumin and bOvine
serum albumin with sulphydryl groups blocked had the same affinitY for allylisothiocyanate
suggesting that amino and sulphydryl groups may not be involved
in the interaction. Polyacrylamide gel electrophoresis and estimation of available
lysine suggested that there were perhaps two types of groups involved in the interaction
of allylisothiocyanate with bovine serum albumin.