{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T05:27:06Z","timestamp":1791264426135,"version":"4.1.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1975,4,1]]},"abstract":"<jats:p>1. Two methods were used to obtain \u03b1-mannosidase free from unbound Zn2+, (a) by removal of excess of metal ion from preparations purified in the presence of Zn2+ and (b) by purification under conditions that eliminate the need to add Zn2+. 2. The purified enzyme is homogeneous on ultracentrifugation, polyacrylamide-gel electrophoresis and gel chromatography. 3. The molecular weight is estimated to be 230 000. 4. The enzyme contains between 470 and 565 mug of zinc\/g of protein, corresponding to between 1.7 and 2 atoms of zinc\/enzyme molecule. The contents of other metals are much lower. 5. The enzyme is inactivated by chelating agents and activity is restored by Zn2+. 6. No other metal ion was found to replace Zn2+ with retention of activity. Some bivalent metal ions, e.g. Cu2+, rapidly inactivate the enzyme. 7. The results indicate that jack-bean \u03b1-mannosidase exists naturally as a zinc-protein complex and may be considered as a metalloenzyme.<\/jats:p>","DOI":"10.1042\/bj1470083","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:57:34Z","timestamp":1439236654000},"page":"83-90","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":59,"title":["Characterization of jack-bean \u03b1-D-mannosidase as a zinc metalloenzyme"],"prefix":"10.1042","volume":"147","author":[{"given":"S M","family":"Snaith","sequence":"first","affiliation":[{"name":"Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/147\/1\/83\/563702\/bj1470083.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/147\/1\/83\/563702\/bj1470083.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T16:18:54Z","timestamp":1637943534000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/147\/1\/83\/9450\/Characterization-of-jack-bean-D-mannosidase-as-a"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1975,4,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1975,4,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1470083","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1975,4,1]]}}}