Polyphenolic protein
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The small family of proteins that are sometimes referred to as polyphenolic proteins are produced by some marine invertebrates like the blue mussel, Mytilus edulis[1] by some algae'[citation needed], and by the polychaete Phragmatopoma californica.[2] These proteins contain a high level of a post-translationally modified—oxidized—form of tyrosine, L-3,4-dihydroxyphenylalanine (levodopa, L-DOPA)[2] as well as the disulfide (oxidized) form of cysteine (cystine).[1] In the zebra mussel (Dreissena polymorpha), two such proteins, Dpfp-1 and Dpfp-2, localize in the juncture between byssus threads and adhesive plaque.[relevant? ][3][relevant? ] The presence of these proteins appear, generally, to contribute to stiffening of the materials functioning as bioadhesives.[4][citation needed] The presence of the dihydroxyphenylalanine-moiety arises from action of a tyrosine hydroxylase-type of enzyme;[citation needed] in vitro, it has been shown that the proteins can be cross-linked (polymerized) using a mushroom tyrosinase.[relevant? ][5]
References
- ↑ 1.0 1.1 Lua error in package.lua at line 80: module 'strict' not found.
- ↑ 2.0 2.1 Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
External links
adhesive_protein,_mussel at the US National Library of Medicine Medical Subject Headings (MeSH)
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