2185 



Pfitzenmeyer, H. T.,and K. C. Drobeck. 1967. 



Some factors influencing reburrowing activity of soft-shell clam Mya 

 arenaria. Chesapeake Sci. 8(3): 193-199. 



It was concluded that many soft clams, Mya arenaria, deposited on the 

 bottom by commercial dredgers, reburrow back into the sediment. Mercenaria 

 mercenaria was not mentioned. - J.L.M. 



2186 



Quin, Louis D. 1965. 



The presence of compounds with a carbon-phosphorus bond in some marine 

 invertebrates. Biochemistry 4(2): 324-330. 



By a difference in total and phosphate phosphorus, the presence of compounds 

 containing the carbon-phosphorus bond was detected in certain fractions 

 derived from 6 marine invertebrates, including Venus mercenaria. V. mer- 

 cenaria, 64 grams wet weight in fraction A had a weight of 1.96 grams, and 

 gave 0.9 7 g total phosphorus, 0.80 g phosphate, and 0.17 g As C-P including 

 aminoethylphosphonic acid; fractions B+C (the insoluble residue from extrac- 

 tion of fraction A) was 10.1 g by weight, and gave 0.37 total phosphorus, 

 and 0.38 phosphate. Relative amounts of C-P material in marine animals in 

 mg P/100 g dry tissue were Tealia felina 410, Metridium dianthus 302, 

 Busycon aanaliculatum 215, Mytilus edulis 76, Asterias forbesi 32, and V. 

 mercenaria 28. V. mercenaria apparently had C-P compounds in fraction A 

 only, and 2-aminoethylphosphonic acid was isolated from the hydrolysates. 

 - J.L.M. 



2187 



Radlick, Lynn, and W. H. Johnson. 1980. 



Paramyosin phosphokinase and phosphatase activity in molluscan muscle 

 extracts. Fed. Proc. 39(6): 2042 (abstract 2302). 



a-paramyosin extracted from adductor muscles of Mercenaria mercenaria con- 

 tains up to 4 moles of phosphate/mole of paramyosin. Removal of phosphate 

 by treatment at pH 12 increases the solubility of paramyosin in the physio- 

 logical range. We attempted isolation of paramyosin phosphokinases and 

 phosphatases from Mercenaria adductor muscles. Early, low salt washes con- 

 tain C-AMP dependent phosphatase activity. Ca++ dependent activity co- 

 precipitates with paramyosin from high salt (0.7 M KC1) extracts. ot- 

 paramyosin purified by modification of the method described by Edwards et al. 

 behaves as if it has intrinsic phosphokinase activity, in that solutions 

 containing paramyosin at concentrations above 1.0 mg/ml show considerable 

 transfer of phosphate from y 32 P-ATP to TCA precipitable protein, i.e., puri- 

 fied paramyosin. Attempts to separate this activity from paramyosin have 

 thus far failed. These results suggest the presence of enzymatic activity 

 capable of either phosphorylation of or removal of phosphate from paramyosin 

 in muscles known to have a catch function. - modified authors' abstract - 

 J.L.M. 



2188 



Rapport, Maurice M.,and Nicholas F. Alonzo. 1960. 



The structure of plasmalogens . V. Lipids of marine invertebrates. J. Biol. 

 Chem. 235(7): 1953-1956. 



Total lipid extracts of tissues from 11 marine invertebrates, including 

 Venus mercenaria, were studied for their content of aldehydogenic lipid and 

 a, g-unsaturated ether. In 8 species the unsaturated ether linkage accounted 

 for almost all the plasmalogen, and in three it accounted for 75% to 85%. 

 Only a small proportion of total plasmalogen was found among choline lipids. 

 The concentration of plasmalogen in lipids of many marine invertebrates is 

 as high as that in lipids of mammalian brain (greater than 10% of the total) . 

 The most suitable animals for further study appear to be Arbacia punctulata 

 and Busycon aanaliculatum. - J.L.M. 



608 



