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Isolation of a glycopeptidase from sweet almond and determination of the N-terminal sequence of its protein moiety
E. N. Kaliberda, V. V. Shemyakin, V. K. Antonov
M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow
Abstract: A glycopeptidase was isolated from sweet almong and purified by a modified approach including hydrophobic chromatography on Butyl-TSK 050 S as the final step. The homogeneous protein (molecular mass 71 kD) was obtained by gel-filtration on Sephacryl S-200, its specific activity being 203 units/mg. The sequence of ten N-terminal amino. acid residues of the enzyme's protein moiety was determined.
Russian Journal of Bioorganic Chemistry 1990, 16 (6):751-758