{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T03:52:28Z","timestamp":1789444348290,"version":"build-2803163510"},"reference-count":19,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[1973,2,1]],"date-time":"1973-02-01T00:00:00Z","timestamp":97372800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[1973,2]]},"abstract":"\n d<\/jats:sc>\n -Arabinose isomerase (EC 5.3.1.3) has been isolated from\n l<\/jats:sc>\n -fucose-induced cultures of\n Escherichia coli<\/jats:italic>\n K-12 and\n d<\/jats:sc>\n -arabinose-induced cultures of\n E. coli<\/jats:italic>\n B\/r. Both enzymes were homogeneous in an ultracentrifuge and migrated as single bands upon disc electrophoresis in acrylamide gels. The\n s<\/jats:italic>\n 20,w<\/jats:sub>\n was 14.5 \u00d7 10\n \u221213<\/jats:sup>\n sec for the\n E. coli<\/jats:italic>\n K-12 enzyme and 14.3 \u00d7 10\n \u221213<\/jats:sup>\n sec for the\n E. coli<\/jats:italic>\n B\/r enzyme. The molecular weight, determined by high-speed sedimentation equilibrium, was 3.55 \u00b1 0.06 \u00d7 10\n 5<\/jats:sup>\n for the\n E. coli<\/jats:italic>\n K-12 enzyme and 3.42 \u00b1 0.04 \u00d7 10\n 5<\/jats:sup>\n for the enzyme isolated from\n E. coli<\/jats:italic>\n B\/r. Both enzyme preparations were active wth\n l<\/jats:sc>\n -fucose or\n d<\/jats:sc>\n -arabinose as substrates and showed no activity on any of the other aldopentoses or aldohexoses tested. With the\n E. coli<\/jats:italic>\n K-12 enzyme, the\n K<\/jats:italic>\n m<\/jats:sub>\n was 2.8 \u00d7 10\n \u22121<\/jats:sup>\n m<\/jats:sc>\n for\n d<\/jats:sc>\n -arabinose and 4.5 \u00d7 10\n \u22122<\/jats:sup>\n m<\/jats:sc>\n for\n l<\/jats:sc>\n -fucose; with the\n E. coli<\/jats:italic>\n B\/r enzyme, the\n K<\/jats:italic>\n m<\/jats:sub>\n was 1.7 \u00d7 10\n \u22121<\/jats:sup>\n m<\/jats:sc>\n for\n d<\/jats:sc>\n -arabinose and 4.2 \u00d7 10\n \u22122<\/jats:sup>\n m<\/jats:sc>\n for\n l<\/jats:sc>\n -fucose. Both enzymes were inhibited by several of the polyalcohols tested, ribitol,\n l<\/jats:sc>\n -arabitol, and dulcitol being the strongest. Both enzymes exhibited a broad plateau of optimal catalytic activity in the alkaline range. Both enzymes were stimulated by the presence of Mn\n 2+<\/jats:sup>\n or Co\n 2+<\/jats:sup>\n ions, but were strongly inhibited by the presence of Cd\n 2+<\/jats:sup>\n ions. Both enzymes were precipitated by antisera prepared against either enzyme preparation. The amino acid composition for both proteins has been determined; a striking similarity has been detected. Both enzymes could be dissociated, by protonation at\n p<\/jats:italic>\n H 2 or by dialysis against buffer containing 8\n m<\/jats:sc>\n urea, into subunits that were homogeneous in an ultracentrifuge and migrated as single bands on disc electrophoresis in acrylamide gels containing urea. The molecular weight of the subunit, determined by high-speed sedimentation equilibrium, was 9.09 \u00b1 0.2 \u00d7 10\n 4<\/jats:sup>\n for the enzyme from\n E. coli<\/jats:italic>\n K-12 and 8.46 \u00b1 0.1 \u00d7 10\n 4<\/jats:sup>\n for the enzyme from\n E. coli<\/jats:italic>\n B\/r. On the basis of biophysical studies, both isomerases appear to be oligomeric proteins consisting of four identical subunits.\n <\/jats:p>","DOI":"10.1128\/jb.113.2.687-696.1973","type":"journal-article","created":{"date-parts":[[2020,1,3]],"date-time":"2020-01-03T13:39:58Z","timestamp":1578058798000},"page":"687-696","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":35,"title":["Properties of\n d<\/scp>\n -Arabinose Isomerase Purified from Two Strains of\n Escherichia coli<\/i>"],"prefix":"10.1128","volume":"113","author":[{"given":"James R.","family":"Boulter","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Section of Biochemistry and Molecular Biology, University of California, Santa Barbara, California 93106"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William O.","family":"Gielow","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Section of Biochemistry and Molecular Biology, University of California, Santa Barbara, California 93106"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1128\/JB.90.4.1157-1158.1965","article-title":"Growth of Aerobacter aerogenes on D-arabinose and L-xylose","volume":"90","author":"Camyre K. P.","year":"1965","unstructured":"Camyre , K. P. , and R. P. Mortlock . 1965 . Growth of Aerobacter aerogenes on D-arabinose and L-xylose . J. Bacteriol. 90 : 1157 - 1158 .","journal-title":"J. Bacteriol."},{"key":"p_2","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1111\/j.1749-6632.1964.tb14213.x","article-title":"Disc electrophoresis. II. Methods and application to human serum protein","volume":"121","author":"Davis B. J.","year":"1964","unstructured":"Davis , B. J. 1964 . Disc electrophoresis. II. Methods and application to human serum protein . Ann. N. Y. Acad. Sci. 121 : 404 .","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"p_3","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/S0021-9258(19)77782-5","article-title":"A new spectrophotometric method for the detection and determination of keto sugars and trioses","volume":"192","author":"Dische Z.","year":"1951","unstructured":"Dische , Z. , and E. J. Borenfreund . 1951 . 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