{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T15:52:28Z","timestamp":1789660348469,"version":"4.0.1"},"reference-count":36,"publisher":"Wiley","license":[{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"funder":[{"DOI":"10.13039\/501100004919","name":"King Abdulaziz City for Science and Technology","doi-asserted-by":"publisher","award":["11-BIO-1516-03"],"award-info":[{"award-number":["11-BIO-1516-03"]}],"id":[{"id":"10.13039\/501100004919","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Evidence-Based Complementary and Alternative Medicine"],"published-print":{"date-parts":[[2015]]},"abstract":"<jats:p>L-asparaginase from bacteria has been used in treatment of acute lymphoblastic leukemia. The aim of this study was to purify and characterize L-asparaginase from<jats:italic>Phaseolus vulgaris<\/jats:italic>seeds instead of microbial sources. L-asparaginase was purified to apparent homogeneity. The enzyme has molecular mass of 79\u2009kDa. The purified asparaginase had very low activity toward a number of asparagine and glutamine analogues. L-asparaginase was free from glutaminase activity. Kinetic parameters, Km and<jats:italic>V<\/jats:italic>max of purified enzyme, were found to be 6.72\u2009mM and 0.16\u2009<jats:italic>\u03bc<\/jats:italic>M, respectively. The enzyme had optimum pH at 8.0. The enzyme showed high stability at alkaline pH (pH 7.5\u20139.0) when incubated for up to 24\u2009h. L-asparaginase had the same temperature optimum and thermal stability at 37\u00b0C. K<jats:sup>+<\/jats:sup>was able to greatly enhance the activity of asparaginase by 150% compared with other metals tested. In conclusion, L-asparaginase showed no glutaminase activity and good stability over a wide range of physiological conditions, and thus it could be used as a potential candidate for treatment of acute lymphoblastic leukemia.<\/jats:p>","DOI":"10.1155\/2015\/309214","type":"journal-article","created":{"date-parts":[[2015,8,27]],"date-time":"2015-08-27T21:32:06Z","timestamp":1440711126000},"page":"1-6","source":"Crossref","is-referenced-by-count":27,"title":["Purification and Characterization of Asparaginase from<i>Phaseolus vulgaris<\/i>Seeds"],"prefix":"10.1155","volume":"2015","author":[{"given":"Saleh A.","family":"Mohamed","sequence":"first","affiliation":[{"name":"Biochemistry Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed F.","family":"Elshal","sequence":"additional","affiliation":[{"name":"Biochemistry Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi 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