ISSN:
1615-6102
Keywords:
Cytomatrix proteins
;
Domain structure
;
Solid phase binding
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary Plectin is a high Mr cytomatrix protein consisting of an elongated rod domain terminated by a globe at each end. Partial proteolysis of plectin by elastase, protease V 8 or trypsin and rotary shadowing electron microscopy of samples revealed mainly filamentous structures, steadily decreasing in length with digestion time. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of elastase- and protease V 8-treated samples revealed a number of fragments from Mr 300,000 to 100,000. These fragments most likely represented intact or large portions of plectin's rod domain, as they were immunoreactive with a monoclonal antibody specific for plectin rods. As shown by electron microscopy, centrifugation, and solid phase binding assays, intact as well as fragmented plectin self-associated via its globular domains; vimentin interaction, on the other hand, occurred via the rod domain. Thus, plectin molecules contain at least two structurally and functionally distinct domains.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01349348
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