and Meroenaria; and benthic phosphate release as 

 0.01 02-5.93, with no significant differences be 

 Over a temp, range from 3.2 to 22.4°C ammonia fl 

 varied from -4.28 to 276.10 |amoles/m 2 /hr . Nitra 

 directions across the sediment-water interface, 

 4 3.43 umoles/m 2 /hr . Nitrite flux was relatively 

 take and release ranged from -9.43 to 41.63 ymol 

 differences were found among the three communiti 

 exerted a strong influence on the fluxes of ammo 

 fluxes measured can have significant effects on 

 the overlying water. - J.L.M. 



a function of oxygen uptake 

 tween the three communities, 

 ux at the sediment surface 

 te was transported in both 

 varying from -66.31 to 

 unimportant. Phosphate up- 

 es/mVhr. Few significant 

 es (p 0.05) . Temperature 

 nia and phosphate. The 

 nutrient concentrations of 



739 



Hall, William R. , Jr. 1979 (?) 



The hard clam. Delaware Marine Adv. 

 College Program 12, 6 p. 



Serv. Publ , 



Univ. Del. Sea Grant 



740 



The name of the hard clam, Meroenaria meroenaria, comes from the Latin 

 mercenari which means "hired for wages" or "Hired one". Covers in brief 

 the biology, commercial and recreational clamming, and shucking and storage 

 of clams. - J.L.M. 



Halsey, John F.,and William F. Harrington. 1973. 



Substructure of paramyosin. Correlation of helix stability, trypsin 

 digestion kinetics, and amino acid .composition. Biochemistry 12(4): 693-701. 



Analysis of kinetics of tryptic proteolysis of paramyosin prepared from 

 adductor muscle of Meroenaria meroenaria suggested that 2 reaction classes 

 were present. Measurements of viscosity and mass during the digestion 

 reaction showed that the fast-reaction class was likely a clustered set of 

 susceptible peptide bonds. A light meromyosin particle, "light paramyosin", 

 was isolated from the proteolytic reaction products at the end of the fast 

 reaction. Paramyosin had a multiphasic "melt" curve, including 2 cooperative 

 transitions with T m values of 44 and 64°. The structure melting at 44° 

 (amounting to about 1/3 of the paramyosin mass) was the region cleaved 

 preferentially to low molecular weight peptides during preparation of light 

 paramyosin. The trypsin-sensitive region was the helical region of low 

 thermal stability. Estimated helix-stabilizing characteristics gave good 

 correlation with observed thermal stabilities. The demonstrated properties 

 of the paramyosin molecule led to hypotheses about its role in the catch 

 mechanism of molluscan muscle. It was suspected that a cooperative phase 

 change in individual molecules may occur in the low thermal stability region 

 during catch. The bonding arrangement of paramyosin in the thick filament 

 core, in which there is a systematic arrangement of gaps between molecules 

 and no end-to-end bonding, could allow a conformational change within 

 individual molecules without affecting specific interactions between overlap 

 regions of neighboring molecules. Thus, the basic 145-A spacing would be 

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



741 



Halstead, B. W. 1972. 



Toxicity of marine organisms caused by pollutants. In 

 Sea Life. Mario Ruivo (ed) Fishing News (Books) Ltd. 



Marine Pollution and 

 , London: 584-594. 



Cites a personal communication from Sister Arline C. Schmeer dated 1 July 1970 

 in which she stated that the anti-tumor substance mercenene, produced by 

 Meroenaria meroenaria under normal conditions, declines in effectiveness when 

 clams are stored in polluted waters. - J.L.M. 



207 



