PURIFICATION OF MYELOPEROXIDASES FROM BONE MARROW OF GUINEA PIG

被引:165
作者
HIMMELHOCH, SR
EVANS, WH
MAGE, MG
PETERSON, EA
机构
[1] Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Department of Health, Department of Education, and Welfare, Bethesda
关键词
D O I
10.1021/bi00831a022
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Myeloperoxidase, an enzyme that appears in the leukocyte during maturation, constitutes a good model system for the study of enzyme differentiation because of its favorable physical and biological properties. A relatively simple method is described for the preparation of this enzyme fromwhite blood cells of guinea pig bone marrow. Electrophoretic and immunological examination of the product indicate that it is suitable for the preparation of immunological reagents to be used in studies of differentiation. The purification procedure also resolves and purifies a second protein with peroxidase activity from this source which differs immunologically, spectrally, and in solubilityfrom the previously described “myeloperoxidases”. © 1969, American Chemical Society. All rights reserved.
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页码:914 / +
页数:1
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