Abstract
The epsilon-amino groups of lysine and phenolic groups of tyrosine are most heavily concentrated in the newlydeposited organic matrix of the shell of the bivalve Mercenaria mercenaria. A phenoloxidase enzyme which oxidizes L-dihydroxyphenylalanine is present only in this “new” area of the shell matrix. Scanning electron micrographs of calcified secretions of the shell show that accretion lines, thought to be layers of organic matrix separating diurnal acceretions of calcium carbonate, are not developed until up to 4 d after deposition of shell material. These results suggest that the shell matrix is hardened by some kind of polymerization, and that lysine and tyrosine residues in the matrix are involved in the process. Accretion lines in polished and etched sections become visible only after complete hardening of the polymer occurs.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Literature Cited
Baker, J. R.: The histochemical recognition of certain guanidine derivatives. Q. Jl microsc. Sci. 88, 115–121 (1947)
Baker, J. R.: The histochemical recognition of phenols, especially tyrosine. Q. Jl microsc. Sci. 97, 161–164 (1956)
Beedham, G. E.: Observations on the non-calcarious component of the shell of the Lamellibranchia. Q. Jl microsc. Sci. 99, 341–357 (1958)
Brown, C. H.: Some structural proteins of Mytilus edulis. Q. Jl microsc. Sci. 93, 487–502 (1952)
Brunet, P. C. J.: Sclerotins. Endeavor 26, 68–74 (1967)
Crenshaw, M. A.: The soluble matrix from Mercenaria mercenaria shell. Biomin. Res. Rep. 6, 6–11 (1972)
Dabbous, M. K.: Inter- and intramolecular cross-linking in tyrosinase-treated tropocollagen. J. biol. Chem. 241, 5307–5312 (1966)
Danielli, J. F.: Studies on the cytochemistry of proteins. Cold Spring Harbor Symp. quant. Biol. 14, 32–39 (1950)
Degens, E. T., D. W. Spencer and R. H. Parker: Paleobiochemistry of molluscan shell proteins. Comp. Biochem. Physiol. 20, 553–579 (1967)
Gordon, J. and M. R. Carriker: Growth lines in a bivalve mollusk: subdaily patterns and dissolution of the shell. Science, N.Y. 202, 519–521 (1978)
Grégoire, C.: Structure of the molluscan shell. In: Chemical Zoology, The Mollusca, pp 45–102. Ed. by M. Florkin and B. T. Scheer. New York: Academic Press 1972
Hackman, R. H.: Chemistry of insect cuticle. II. The water-insoluble proteins of the cuticle of Aphodius howitti Hope (Coleoptera). Biochem. J. 54, 367–370 (1953a)
Hackman, R. H.: Chemistry of insect cuticle. III. Hardening and darkening of the cuticle. Biochem. J. 54, 371–377 (1953b)
Hackman, R. H. and A. R. Todd: Some observations on the reaction of catechol derivatives with amines in the presence of oxidizing agents. Biochem. J. 55, 631–637 (1953)
Hare, P. E.: Amino acids in the proteins from aragonite and calcite in the shells of Mytilus californianus. Science, N.Y. 139, 216–217 (1963)
Kawasaki, H., H. Sato and M. Suzuki: Structural proteins in the egg envelopes of dragonflies, Sympetrum infuscatum and S. frequens. Insect Biochem. 4, 99–111 (1974)
Lerner, A. B., T. B. Fitzpatrick, E. Calkins and W. H. Summerson: Mammalian tyrosinase: preparation and properties. J. biol. Chem. 178, 185–195 (1949)
Lillie, R. D.: Histopathologic technic and practical histochemistry. New York: McGraw-Hill 1965
Lison, L.: Histochimie et cytochimie animales. Paris: Gauthier-Villars 1960
Meenakshi, V. R., P. E. Hare, N. Watabe and K. M. Wilbur: The chemical composition of the periostracum of the molluscan shell. Comp. Biochem. Physiol. 29, 611–620 (1969)
Pannella, G. and C. MacClintock: Biological and environmental rhythms reflected in molluscan shell growth. Paleont. Soc. Mem. 2, 64–80 (1968)
Pryor, M. G.: On the hardening of the cuticle in insects. Proc. R. Soc. (London) 128B, 378–393 (1940)
Rosselet, A. and F. Ruch: Cytofluorometric determination of lysine with dansychloride. J. Histochem. Cytochem. 16, 459–465 (1968)
Saleuddin, A. S. M. and P. E. Hare: Amino acid composition of normal and regenerated shell of Helix. Can. J. Zoo. 48, 886–888 (1970)
Sizer, I. W.: Oxidation of proteins by tyrosinase and peroxidase. Adv. Enzymol. 14, 129–161 (1953)
Sizer, I. W. and P. F. Wagley: The action of tyrosinase on thrombin, firbinogen, and fibrin. J. biol. Chem. 192, 213–221 (1951)
Smyth, J. D.: A technique for the histochemical demonstation of polyphenol oxidase and its application to egg-shell form-ation in helminths and byssus formation. Q. Jl microsc. Sci. 95, 139–152 (1954)
Stevenson, J. R. and T. Y. Adomako: Diphenol oxidase in the crayfish cuticle. Localization and changes in activity during the molting cycle. J. Insect Physiol. 13, 1803–1811 (1967)
Taylor, J. D., W. J. Kennedy and A. Hall: The shell structure and mineralogy of the Bivalvia. Introduction: Nuculacea and Trigonacea. Bull. Br. Mus. nat. Hist., Zool. Suppl. 3, 1–125 (1969)
Thompson, S. W.: Selected histochemical and histopathological techniques, 1639 pp. Springfield, Ill: Charles C. Thomas 1966
Weiner, S. and L. Hood: Soluble protein of the organic matrix of mollusk shells: a potential template for shell formation. Science, N.Y. 190, 987–989 (1975)
Yamuma, A. and T. Ichikawa: Ninhydrin-Schiff and Alloxan-Schiff staining. Lab. Clin. Med. 41, 296–299 (1953)
Author information
Authors and Affiliations
Additional information
Communicated by I. Morris, West Boothbay Harbor