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Journal of Experimental Biology, Vol 198, Issue 3 633-644, Copyright © 1995 by Company of Biologists
JOURNAL ARTICLES |
X Qin and JH Waite
College of Marine Studies, University of Delaware, Newark 19716.
Byssal threads of the common mussel Mytilus edulis contain collagenous molecules from which two pepsin-resistant fragments have been isolated and characterized. These show a complementary distribution along the length of the thread, such that one predominates distally (Col-D) and the other proximally (Col-P). Both fragments contain three identical alpha-like chains with molecular masses of 50 kDa (Col-P) and 60 kDa (Col-D) and have typically collagenous amino acid compositions; for example, 35% glycine and almost 20% proline plus 4-trans-hydroxyproline. Hydroxylysine and 3-hydroxyproline were absent. Col-P sequences are also typical of collagen in consisting of tandem repeats of the triplet Gly-X-Y in which X and Y generally represent any amino acid. When proline occurs, it is hydroxylated to 4-trans-hydroxyproline only in the Y position. Seven instances where X is glycine have been detected in Col-P. Specific polyclonal anti-Col antibodies were used to isolate the precursors of Col-P and Col-D from the mussel foot. PreCol-P has a molecular mass of 95 kDa and contains 36% glycine but a lower imino acid content (13%). It has a complementary distribution with another precursor (preCol-D, 97 kDa) along the length of the foot. The two precursor compositions suggest resilin-like and silk-fibroin-like structures, respectively, in the noncollagenous domains of preCol-P and preCol-D. Immunogold labelling studies indicate that Col-P is associated with the coiled fibers of the inner core in the proximal portion of the thread, whereas Col-D is localized to the straight fiber bundles of the distal thread as well as to the outer core of the proximal thread.
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  C. Sun and J. H. Waite Mapping Chemical Gradients within and along a Fibrous Structural Tissue, Mussel Byssal Threads J. Biol. Chem., November 25, 2005; 280(47): 39332 - 39336. [Abstract] [Full Text] [PDF]
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 J. M. Lucas, E. Vaccaro, and J. H. Waite A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis J. Exp. Biol., June 15, 2002; 205(12): 1807 - 1817. [Abstract] [Full Text] [PDF]
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K. Coyne and J. Waite In search of molecular dovetails in mussel byssus: from the threads to the stem J. Exp. Biol., January 5, 2000; 203(9): 1425 - 1431. [Abstract] [PDF]
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 X.-X. Qin and J. H. Waite A potential mediator of collagenous block copolymer gradients in mussel byssal threads PNAS, September 1, 1998; 95(18): 10517 - 10522. [Abstract] [Full Text] [PDF]
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X.-X. Qin, K. J. Coyne, and J. H. Waite Tough Tendons. MUSSEL BYSSUS HAS COLLAGEN WITH SILK-LIKE DOMAINS J. Biol. Chem., December 19, 1997; 272(51): 32623 - 32627. [Abstract] [Full Text] [PDF]
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V. V. Papov, T. V. Diamond, K. Biemann, and J. H. Waite Hydroxyarginine-containing Polyphenolic Proteins in the Adhesive Plaques of the Marine Mussel Mytilus edulis J. Biol. Chem., August 25, 1995; 270(34): 20183 - 20192. [Abstract] [Full Text] [PDF]
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