Tidal oscillations at the head of Monterey Submarine Canyon and their relation to oceanographic sampling and the circulation of water in Monterey Bay. Annual report, Part 6, September 1972

During a 25-hour hydrographic times series at two stations near the head of Monterey Submarine Canyon, an internal tide was observed with an amplitude of 80 to 115 m in water depths of 120 and 220 m respectively. These large oscillations produced daily variations in hydrographic and chemical parameters that were of the same magnitude as seasonal variations in Monterey Bay. Computed velocities associated with the internal tide were on the order of 10 em/sec, and this tidally induced circulation may have a significant role in the exchange of deep water between Monterey Submarine Canyon and the open ocean. (PDF contains 49 pages)

Proceedings of the Nineteenth Annual Symposium on Sea Turtle Conservation and Biology, 2-6 March 1999 South Padre Island, Texas, U.S.A.

The 19th Annual Symposium on Sea Turtle Biology and Conservation was the largest to date. The beautiful venue was the South Padre Island Convention Centre on South Padre Island, Texas from March 2-6, 1999. Key features of the 19th were invited talks on the theme The Promise, the Pain, and the Progress of 50 years of Sea Turtle Research and Conservation, a mini-symposium on the Kemp's ridley and an increased emphasis on high quality poster sessions. Hosts for the meeting included Texas A&M University, the Texas Sea Grant College Program, The Gladys Porter Zoo and Sea Turtle, Inc. Co-sponsors included the National Marine Fisheries Service-Southeast Fisheries Science Center, the National Marine Fisheries Service-Protected Resources Branch, Padre Island National Seashore and the U.S. Fish and Wildlife Service. With the assistance of Jack Frazier, we were fortunate to obtain a $30,000 grant from the David and Lucile Packard Foundation. This grant provided travel support to 49 individuals from 24 nations who presented a total of 50 presentations. (PDF contains 309 pages)

Purification and properties of Aspartate aminotransferase (E.C. 2.6.1.1) from skeletal muscle of Cirrhina mrigala

Aspartate aminotransferase (E.C. 2.6.1.1.) from the skeletal muscle of fresh water fish Cirrhina mrigala has been purified 40 fold by ammonium sulphate fractionation, adsorption on alumina Csub(8) gel and chromatography using DEAE-cellulose column and the properties of the purified enzyme studied. The pH optimum of the enzyme is 7.8. The Km value of aspartic acid and 2-oxoglutaric acid are found to be 2.8 x 10sub(-3) M and 1.0 x 10sub(-4) M respectively. The activity of enzyme is inhibited by p-chloromercurybenzoate, hydroxylamine hydrochloride and sodium cyanide. The inhibition by pchloromercurybenzoate is reversed by reduced glutathione, B-mercaptoethanol and cysteine. Dicarboxylic acids such as maleic acid, malic acid and succinic acid inhibit the enzyme activity. The enzyme is not activated by any of the metal ions tested and heavy metal ions such as mercury and silver strongly inhibit the enzyme activity.