IN-SITU LOCALIZATION OF THE 60-K PROTEIN OF HELICOBACTER-PYLORI, WHICH BELONGS TO THE FAMILY OF HEAT-SHOCK PROTEINS, BY IMMUNOELECTRON MICROSCOPY

被引：25

作者：

ESCHWEILER, B

BOHRMANN, B

GERSTENECKER, B

SCHILTZ, E

KIST, M

机构：

[1] UNIV BASEL,BIOZENTRUM,DEPT BIOPHYS CHEM,CH-4000 BASEL,SWITZERLAND

[2] INST VIRION,W-8700 WURZBURG,GERMANY

[3] UNIV FREIBURG,INST ORGAN CHEM & BIOCHEM,D-79104 FREIBURG,GERMANY

来源：

ZENTRALBLATT FUR BAKTERIOLOGIE-INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY VIROLOGY PARASITOLOGY AND INFECTIOUS DISEASES | 1993年 / 280卷 / 1-2期

关键词：

D O I：

10.1016/S0934-8840(11)80942-4

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The groEl homologue of Helicobacter pylori was isolated and characterized by means of immunoelectron microscopy, after cryosectioning. The 60 k protein was isolated from Helicobacter pylori by treatment of the cells with 2-butanol and purified by anion exchange chromatography. The native molecular weight of the 60 k protein was estimated to be 420 k by size exclusion chromatography. The purified 60 k protein showed the typical rotational symmetry of chaperonins when analyzed by electron microscopy. Ultrathin sections of Helicobacter pylori were immunostained by a polyclonal antibody directed against the hsp-65 of Mycobacterium tuberculosis. The label revealed a clustered localization of the 60 k protein on the cell surface as well as in the periplasmic space.

引用

页码：73 / 85

页数：13

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