HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vallee, R. B. Articles by Borisy, G. G. Search for Related Content PubMed PubMed Citation Articles by Vallee, R. B. Articles by Borisy, G. G. Social Bookmarking                      What's this?

JBC, Vol. 252, Issue 1, 377-382, Jan, 1977

Removal of the projections from cytoplasmic microtubules in vitro by digestion with trypsin

R. B. Vallee and G. G. Borisy

Trypsin was found to selectively destroy the high molecular weight (HMW) proteins associated with microtubules. Both major groups of high molecular weight bands observed by sodium dodecylsulfate-polyacrylamide gel electrophoresis were destroyed at the same rate (t 1/2 = 1 min), while tubulin was little affected under the conditions employed. Destruction of the high molecular weight bands was correlated with the disappearance of the lateral projections observed on the surface of microtubules. The trypsin-treated protein was capable of reassembly to form microtubules and showed characteristic ring-shaped structures at low temperature. Analysis of fragments formed from the high molecular weight proteins indicated the initial appearance of a fragment of M = 255,000 which failed to bind to microtubules. These results suggest that a small fragment of the high molecular weight protein molecule may remain bound to the microtubule after removal of the lateral projection, and that this fragment may retain the ability to promote microtubule assembly.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K. Tokuraku, K. Matsushima, T. Matui, H. Nakagawa, M. Katsuki, R. Majima, and S. Kotani The Number of Repeat Sequences in Microtubule-associated Protein 4 Affects the Microtubule Surface Properties J. Biol. Chem., August 8, 2003; 278(32): 29609 - 29618. [Abstract] [Full Text] [PDF]

				N. E. Ziv and M. E. Spira Induction of Growth Cone Formation by Transient and Localized Increases of Intracellular Proteolytic Activity J. Cell Biol., January 12, 1998; 140(1): 223 - 232. [Abstract] [Full Text] [PDF]

				U Preuss, J Biernat, E. Mandelkow, and E Mandelkow The 'jaws' model of tau-microtubule interaction examined in CHO cells J. Cell Sci., January 3, 1997; 110(6): 789 - 800. [Abstract] [PDF]

				M. A. DeTure, E. Y. Zhang, M. R. Bubb, and D. L. Purich In Vitro Polymerization of Embryonic MAP-2c and Fragments of the MAP-2 Microtubule Binding Region into Structures Resembling Paired Helical Filaments J. Biol. Chem., December 20, 1996; 271(51): 32702 - 32706. [Abstract] [Full Text] [PDF]

				R. L. Coffey and D. L. Purich Non-cooperative Binding of the MAP-2 Microtubule-binding Region to Microtubules J. Biol. Chem., January 20, 1995; 270(3): 1035 - 1040. [Abstract] [Full Text] [PDF]

				B. Weisshaar, T. Doll, and A. Matus Reorganisation of the microtubular cytoskeleton by embryonic microtubule-associated protein 2 (MAP2c) Development, December 1, 1992; 116(4): 1151 - 1161. [Abstract] [PDF]

				P Sherline and K Schiavone Immunofluorescence localization of proteins of high molecular weight along intracellular microtubules Science, December 9, 1977; 198(4321): 1038 - 1040. [Abstract] [PDF]