首页   按字顺浏览 期刊浏览 卷期浏览 Immunological comparison of 22S, 19S, and 12S dyneins fromParameciumcilia
Immunological comparison of 22S, 19S, and 12S dyneins fromParameciumcilia

 

作者: Claire E. Walczak,   Silvio P. Marchese‐Ragona,   David L. Nelson,  

 

期刊: Cell Motility and the Cytoskeleton  (WILEY Available online 1993)
卷期: Volume 24, issue 1  

页码: 17-28

 

ISSN:0886-1544

 

年代: 1993

 

DOI:10.1002/cm.970240103

 

出版商: Wiley Subscription Services, Inc., A Wiley Company

 

关键词: antibody;motility;axoneme;ATPase

 

数据来源: WILEY

 

摘要:

AbstractThree forms of dynein (22S, 19S, and 12S) were purified fromParameciumcilia. Two classes of monoclonal antibodies against purified 22S dynein were generated. One class reacted on immunoblots with the heavy chains of 22S, 19S, and 12S dyneins; the second class reacted with an 88 kD intermediate chain of 22S dynein. Polyclonal antiserum to the heavy chains of 22S dynein reacted with the γ‐heavy chain of 22S and 19S dyneins. A previously described antiserum raised against 22S dynein [Travis et al.: Biochim. Biophys. Acta 966:73–83, 1988] recognized the γ‐heavy chain of 22S dynein which was also present in 19S and 12S dyneins, along with the 88 and 76 kD intermediate chains of 22S dynein. This antiserum was also able to immunoprecipitate dynein from crude extracts of cilia.Electron microscopy revealed that the 22S dynein consisted mainly of two‐headed particles with some three‐headed particles present. The 12S dynein was mainly one‐headed particles. The 19S dynein was a mixture of three‐, two‐, and one‐headed particles. The immunological and electron microscopic studies showed that 19S dynein arises from 22S dynein, and that 12S dynein is heterogeneous, composed of the γ‐heavy chain of 22S dynein and a unique dynein ATPase.The polyclonal antibodies were also used to detect cross‐reactive proteins in other organisms. Both the anti‐heavy chain and the anti‐22S dynein sera reacted strongly with 22S outer arm dynein ofTetrahymena, but not with the 14S dynein of this orga

 

点击下载:  PDF (1210KB)



返 回