ammonium sulfate; 2) inactivated by extraction with chloroform, but not with 

 toluene or xylene; and 3) inactivated by chymotrypsin and protease, but not 

 by deoxyribonuclease. Electrophoretic analysis shows that the agglutinin 

 is composed of subunits each with a molecular weight of approximately 21,000. 

 Calcium ions are required for the activity of agglutinin and contribute to 

 heat stability of the molecule. Several saccharides, which may constitute 

 a portion of the bacterial agglutinin receptors, were able to partially in- 

 hibit agglutination. In vitro studies using clam hemocytes showed that the 

 phagocytosis of a marine bacterium, designated as RS-005, was enhanced by 

 the presence of hemolymph. Adsorption of hemolymph samples with RS-005 

 bacteria removed the agglutinin activity for all types of cell tested and 

 also abolished the opsonic effect. Further information on the roles of 

 these substances in vivo is needed to clarify their biological significance. 

 - modified authors' abstract - J.L.M. 



2084 



Avault, James W. , Jr. 1980. 



Aquaculture. Chapter 16 in Fisheries Management. Robert T. Lackey and 

 Larry A. Nielsen (eds.) . John Wiley & Sons, New York: 379-411. 



Hard clam or quahog (Meraenaria meraenaria) is found along the Atlantic 

 coast of the United States from Maine to Florida in the intertidal zone to 

 water as deep as 15 meters. Hard clam can be farmed using procedures sim- 

 ilar to those used for oysters. They do not require cultch on which to 

 settle. Crushed stone or gravel can be placed on the bottom, so that clams 

 are safe from predatory crabs and fish. Clams can be dredged, or harvested 

 with hoes and hand labor. Clam culture is not widespread. - J.L.M. 



2085 



Ayres, David C.,and Gary R. W. Denton. 1975. 



On the diversity of products obtained during synthesis of polychlorobiphenyls 

 by the Van Roosmalen procedure. Bull. Envir. Contam. Toxicol. 14(3): 361-369. 



Polychlorobiphenyls were required for in vivo toxicity testing with the hard 

 clam Meraenaria meraenaria , and the importance of pure substrates for this 

 work has already been stressed. - J.L.M. 



2086 



Ayres, P. A. 19 78. 



Shellfish purification in installations using UV light. Gt. Britain Min. 

 Agric. Food Fish., Dir. Fish. Res. Lab., Leaflet 43: 1-20. 



Detailed reference to Meraenaria meraenaria unlikely. Did not search 

 beyond SUNY-Stony Brook library. - J.L.M. 



2087 



Bagshaw, Clive R., and John Kendrick- Jones . 1980. 



Identification of the divalent metal ion binding domain of myosin regula- 

 tory light chains using spin-labelling techniques. J. Mol. Biol. 140(3): 

 411-433. 



By the criterion of their primary structure myosin regulatory light chains 

 belong to the "calcium binding protein" family and are thought to contain 

 domains related to the E-F hand structure found in parvalbumin. However, 

 the presence of deletions and non-conservative substitutions in the reg- 

 ulatory light chains indicates that, of the four domains apparent in their 

 structure, only the first is competent to bind Ca ++ or other divalent 

 metal ions. Electron paramagnetic resonance studies were performed in an 

 attempt to provide experimental verification of this hypothesis. The 

 approach is based on the finding that the paramagnetic Mn ++ ion substitutes 

 for Ca ++ at the divalent metal ion site and that different regulatory light- 

 chain isotypes contain cysteine residues in different domains which may be 

 spin-labelled with a nitroxide derivative. The electron spin interaction 

 between these two paramagnetic centers is a function of the distance of 

 their separation. Clam (Meroenaria mercenaria) regulatory light chain 



579 



