1,721,136 research outputs found

    A distinct beta-hexosaminidase isoenzyme separated from human leukemic lymphocytes and myelocytes

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    The beta-hexosaminidase (EC 3.2.1.30) isoenzymes were separated on the basis of their carbohydrate moieties by an affinity chromatography using immobilized phenylboronate. Normal lymphocytes and granulocytes contain two major forms of beta-hexosaminidase, acute lymphoblastic, acute myeloblastic, chronic lymphocytic and chronic myelocytic leukemic cells contain an extra, distinct isoenzyme of beta-hexosaminidase. This extra isoenzyme may be a marker for the leukemic conversion of hematopoietic tissue

    Expression of a particular beta-N-acetylglucosaminidase isoenzyme in human haematopoietic leukemic cell-lines.

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    N-acetyl-beta-D-glucosaminidase (NAG) activity and isoenzyme profiles were studied in myeloid, histiocytic, B-lymphoid, T-lymphoid and lymphoblastoid continuous cell lines in order to determine if N-acetyl-beta-D-glucosaminidase isoenzyme expression may help to distinguish among various types of leukemic proliferation. Total NAG activity in myeloid, histiocytic, erythroleukemic cell lines were higher than Burkitt's lymphoma derived cell lines (B-lymphoid), T- or lymphoblastoid cell lines. On chromatofocusing by PBE 94 coupled with an automated enzyme assay an intermediate (I) beta-N-acetyl-glucosaminidase form, eluting between forms B and A, was found in all leukemic and in Epstein-Barr virus infected lymphoblastoid cell lines analysed. The different profiles recorded, the expression of the I form and the different I/B ratios may be useful as markers of tumour proliferation
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