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Purification and Partial C-terminal Amino Acids Sequencing of -glucosidase from Munor Javanicus

P. M. Kutima

出版	Universiti Pertanian Malaysia, 1994
URL	http://books.google.com.hk/books?id=uet7AQAACAAJ&hl=&source=gbs_api

註釋

-Glucosidase (EC 3.2.1.20) from Mucor javanicus was purified to homogencity. Monospecificantibody was raised against purified enzyme rabbit. The antibody was immobilised on 2-fluoro-1-methylpyridium-toluene-4-sulfonate activated cellulofine and an antigen eluted through the antibody packed column. Analysis of the purified protein by denaturing gel electrophoresis revealed a single polypeptide with an apparent molecular weight or 99,000. Immunological analyses showed that the antibody reacted with only the enzyme. The purified enzyme was digested with trifluoroacetic acid, tryptic peptides separated by HPLC and the amino acids partially sequenced from the C-terminal end. [Authors' abstract].