GUINEA-PIG HETEROPHIL AND EOSINOPHIL PEROXIDASE
GUINEA-PIG HETEROPHIL AND EOSINOPHIL PEROXIDASE
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DOI:
10.1016/0003-9861(72)90164-6
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发表时间:
1972-01-01
影响因子:
3.9
通讯作者:
HIMMELHO.R
中科院分区:
文献类型:
--
作者:
DESSER, RK;EVANS, WH;HIMMELHO.R
Guinea pig heterophil and eosinophil peroxidases were purified from bone marrow leukocytes in order to compare certain physical properties. Purified heterophil peroxidase (homogeneous in the ultracentrifuge, by immunologic test, and by gel electrophoresis) had a Soret maximum at 437 nm, an A 437 A 280 ratio of 0.79, and a mol wt of 137,000. The molecule consisted of two subunits of similar size, as assessed by its appearance in the electron microscope and by electrophoresis in SDS polyacrylamide gels. Eosinophil peroxidase required the cationic detergent cetyltrimethylammonium bromide to prevent binding to the materials used in its purification. The purified esoinophil enzyme, homogeneous by immunologic criteria, was resolved by gel filtration into two peroxidase components having mol wts of 75,000 and 150,000, respectively. Each component had the same specific activity, absorption spectrum (Soret maximum at 425 nm), and A 415 A 280 ratio (0.83). Treatment of each with SDS and mercaptoethanol produced a single component with a mol wt of about 65,000. Examination of crude bone marrow extracts resolved only one eosinophil peroxidase component with a mol wt of about 80,000, indicating that aggregation occurred during purification. The leukocyte peroxidases, therefore, have substantially different properties despite their location in analogous organelles of closely related cells.