By Mehmet Sarikaya (auth.), Professor Dr. Steven T. Case (eds.)
ISBN-10: 354047207X
ISBN-13: 9783540472070
ISBN-10: 3662224402
ISBN-13: 9783662224403
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H. Waite unpubl. results). Attempts to find the precursor enzyme in the mussei foot suggest that in both species catecholoxidase exists as a zymogen or latent enzyme prior to secretion. Activation can be effected in vitro by treatment with 38 J. Herber! Waite cr-chymotrypsin which may or may not resemble the natural activator (Waite 1985). Since enzyme activity is latent in the accessory gland, histochemical detection as reported by Smyth (1954) and others should not have been possible unless inadvertant activation during routine fixation and/or dehydration had occurred.
Including the byssus with stern (5). cufT(C), thread (7). and plaque (P). (Waite 1983) composite byssus. , 3,4-dihydroxyphenylalanine or DOPA, the collagen gland eontains collagenous and elastic proteins, the accessory gland stock piles both catecholoxidase activity as weil as o-diphenolic precursors, and the stern gland secretes the lamellar proteins of the stern (Brown 1952; Srnyth 1954; Gerzeli 1961; Pujol 1967; Banu et al. 1980). The mucous glands are located near the tip of the foot and along the margins ofthe ventral groove.
The DOPA and lysine may form a covalent cross-link following the oxidation of the former to an o-quinone (Waitc I 990b), but characterization of specific cross-links has been elusive. The sccond DOPA-protein, so-called MeFP-2, has only recently come to light (Rzepecki LM and Waitc JH, unpub!. results). It has an apparent molecular weight of 42-45 kDa and a pI of about 8. Like the polyphenolic protein, it has a high proportion of lysine and imino acids but no hydroxyproline. DOPA is generally low (2-3 mol%), and cystine (7 mol%), aspartate/asparagine (15 mol%), and glycine (18 molO;;,) levels are high.
Structure, Cellular Synthesis and Assembly of Biopolymers by Mehmet Sarikaya (auth.), Professor Dr. Steven T. Case (eds.)
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