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Differentiation Associated Changes in Isozyme Expression of Amino Acid Naphthylamidase in Myeloid Cells
Author(s) -
Roos G.
Publication year - 1982
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1982.tb00560.x
Subject(s) - isozyme , enzyme , myeloid , haematopoiesis , affinity chromatography , biochemistry , trypsin , biology , amino acid , cell culture , microbiology and biotechnology , chemistry , stem cell , immunology , genetics
Triton X‐100 resistant isozymes of amino acid naphthylamidase were studied by polyacryla‐mide gel electrophoresis, gel filtration and affinity chromatography in samples from 12 human haematopoietic cell lines, 8 leukaemic patients and 4 healthy persons. Affinity to WGA‐Sepharose seemed to be correlated to differentiation in the myeloid series, indicating differences in the N‐acetyl‐glucose‐amine content of the enzyme molecules in mature and immature cells. A high carbohydrate content might be characteristic for mature myeloid cells. By trypsin digestion of intact cells and analysis of released enzyme activities into the medium new information on isozyme expression of amino acid naphthylamidase in the granulocyte‐monocyte lineages could be achieved.