NDLI: Tyrosinases from crustaceans form hexamers.

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Tyrosinases from crustaceans form hexamers.

Content Provider	Semantic Scholar
Author	Jaenicke, Elmar Decker, Heinz
Copyright Year	2003
Abstract	Tyrosinases, which are widely distributed among animals, plants and fungi, are involved in many biologically essential functions, including pigmentation, sclerotization, primary immune response and host defence. In the present study, we present a structural and physicochemical characterization of two new tyrosinases from the crustaceans Palinurus elephas (European spiny lobster) and Astacus leptodactylus (freshwater crayfish). In vivo, the purified crustacean tyrosinases occur as hexamers composed of one subunit type with a molecular mass of approx. 71 kDa. The tyrosinase hexamers appear to be similar to the haemocyanins, based on electron microscopy. Thus a careful purification protocol was developed to discriminate clearly between tyrosinases and the closely related haemocyanins. The physicochemical properties of haemocyanins and tyrosinases are different with respect to electronegativity and hydrophobicity. The hexameric nature of arthropod tyrosinases suggests that these proteins were the ideal predecessors from which to develop the oxygen-carrier protein haemocyanin, with its allosteric and co-operative properties, later on.
Starting Page	5450
Ending Page	5454
Page Count	5
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/371/2/515.full.pdf
PubMed reference number	12466021v1
Volume Number	371
Part	2
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Subject Keyword	Arthropods Astacoidea Astacus Carrier Proteins Family Palinuridae (organism) Freshwater Biology Molecular Mass Oxygen Pigmentation Subphylum Crustacea hyperglycemic hormone precursor, crustacean
Content Type	Text
Resource Type	Article

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