{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T23:19:42Z","timestamp":1792192782740,"version":"4.4.0"},"reference-count":42,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,2,1]]},"abstract":"<jats:p>Exoglycosidases are hydrolases involved in lysosomal degradation of oligosaccharide chains of glycoconjugates (glycoproteins, glycolipids and proteoglycans). In tissues and body fluids, a higher exoglycosidase specific activity is found in N-acetyl-\u03b2-hexosaminidase, than \u03b2-glucuronidase, \u03b1-L-fucosidase, \u03b2-galactosidase, \u03b1-mannosidase and \u03b1-glucosidase. Determination of exoglycosidases (especially N-acetyl-\u03b2-hexosaminidase and \u03b2-glucuronidase) in body fluids could be an inexpensive, easy to perform and sensitive test for pathological evaluation, as well as in screening and monitoring many diseases, including alcohol abuse, risk of arteriosclerosis, bacterial infections (e.g. Lyme borreliosis), chronic inflammatory processes, such as rheumatoid arthritis and juvenile idiopathic arthritis, asthma, autoimmune hepatitis and primary biliary cirrhosis, as well as cancers.<\/jats:p>","DOI":"10.1042\/bst0390406","type":"journal-article","created":{"date-parts":[[2011,1,26]],"date-time":"2011-01-26T12:25:37Z","timestamp":1296044737000},"page":"406-409","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["Exoglycosidase markers of diseases"],"prefix":"10.1042","volume":"39","author":[{"given":"Sylwia","family":"Chojnowska","sequence":"first","affiliation":[{"name":"Medical Institute, College of Computer Science and Business Administration, 18-400 \u0141om\u017ca, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alina","family":"K\u0119pka","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Experimental Medicine, the Children's Memorial Health Institute, 04-730, Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S\u0142awomir\u00a0Dariusz","family":"Szajda","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Biochemistry, Medical University, 15-230 Bia\u0142ystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Napoleon","family":"Waszkiewicz","sequence":"additional","affiliation":[{"name":"Department of Psychiatry, Medical University, 16-070 Bia\u0142ystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcin","family":"Bier\u0107","sequence":"additional","affiliation":[{"name":"Department of Stomatological Surgery, Medical University, 15-276 Bia\u0142ystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krzysztof","family":"Zwierz","sequence":"additional","affiliation":[{"name":"Medical Institute, College of Computer Science and Business Administration, 18-400 \u0141om\u017ca, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2011,1,19]]},"reference":[{"key":"2021111900031463800_B1","doi-asserted-by":"crossref","first-page":"739","DOI":"10.18388\/abp.1999_4146","article-title":"Isoenzymes of N-acetyl-\u03b2-hexosaminidase","volume":"46","author":"Zwierz","year":"1999","journal-title":"Acta Biochim. 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