LOCALIZATION OF THE BINDING-SITE OF AN ANTIBODY AFFECTING ATPASE ACTIVITY OF CHAPERONIN CPN60 FROM BORDETELLA-PERTUSSIS

被引：4
作者：
CEJKA, Z
GOULDKOSTKA, J
BURNS, D
KESSEL, M
机构：
[1] HEBREW UNIV JERUSALEM,HADASSAH MED SCH,DEPT MEMBRANE & ULTRASTRUCT RES,IL-91010 JERUSALEM,ISRAEL
[2] MAX PLANCK INST BIOCHEM,W-8033 MARTINSRIED,GERMANY
[3] US FDA,DIV BACTERIAL PROD,BETHESDA,MD 20892
[4] UNIV MARYLAND,DEPT MICROBIOL,COLL PK,MD 20742
来源：
JOURNAL OF STRUCTURAL BIOLOGY | 1993年 / 111卷 / 01期
关键词：
D O I：
10.1006/jsbi.1993.1033
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：
Imaging processing has revealed the attachment site of antibody 54G8 on chaperonin 60 (cpn60) from Bordetella pertussis. This antibody, previously shown to affect the ability of chaperonin 10 (cpn10) to inhibit the ATPase activity of cpn60, is attached at the ends of the cpn60 and links the molecules into long chains. When only Fab fragments, which also affect ATPase activity, are used for labeling, these attach to both ends of the cpn60 molecule, but the long chains are not seen. Some perturbation of cpn60 was seen when Fab fragments were bound (Fab:cpn60 = 28:1). © 1993 Academic Press, Inc.
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页码：34 / 38
页数：5
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