IDENTIFICATION OF ELASTASE IN HUMAN EOSINOPHILS - IMMUNOLOCALIZATION, ISOLATION, AND PARTIAL CHARACTERIZATION

被引：45

作者：

LUNGARELLA, G ^{[1
]}

MENEGAZZI, R ^{[1
]}

GARDI, C ^{[1
]}

SPESSOTTO, P ^{[1
]}

DESANTI, MM ^{[1
]}

BERTONCIN, P ^{[1
]}

PATRIARCA, P ^{[1
]}

CALZONI, P ^{[1
]}

ZABUCCHI, G ^{[1
]}

机构：

[1] UNIV TRIESTE,INST GEN PATHOL,I-34127 TRIESTE,ITALY

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1992年 / 292卷 / 01期

关键词：

D O I：

10.1016/0003-9861(92)90060-A

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：

Although an elastolytic activity in eosinophil-rich cell fractions from mice has been reported, this enzyme has not been purified and characterized as yet in any mammalian species. Eosinophilic elastase was isolated from human eosinophil fragments (cytosomes) obtained from normal and eosinophilic subjects. The enzyme was purified to apparent electrophoretic homogeneity by fast protein liquid chromatography. The enzyme shows the same physical properties of the major elastase isoenzyme of human neutrophils. In addition, like monocyte elastase, it reacts with a monoclonal antibody against human neutrophil elastase. The biochemical similarities observed between the above-mentioned enzymes and the immunolocalization findings strongly support the idea that human eosinophils and neutrophils contain the same enzyme activity. Eosinophils show immunoreactive material in both types of dense cytoplasmic granules. This observation supports the current hypothesis that the different types of eosinophilic granules represent successive morphological stages of maturation. © 1992.

引用

页码：128 / 135

页数：8

共 45 条

[1] PARTIAL-PURIFICATION AND PROPERTIES OF PORCINE PANCREATIC ELASTASE II [J].