The Km value for meotartaric acid in this system is high, 1-4 x 1O-2M, compared with the Km value for DL-malate, 6-2 x 10-3M. The Km value found for DPN was approximately 5 x 10-3M. None of the carboxylic acids tested as potential inhibitors ofDLmalate oxidation were found to inhibit mesotartaric acid oxidation in pigeon-liver extracts. Similarly, addition of me8otartrate to rat-liver mitochondria resulted in an increased rate of oxygen uptake but much lower activities were found with rat-kidney mitochondria. DISCUSSION Sodium DL-malate is oxidized anaerobically by ferricyanide in the presence of pigeon-liver extracts. The oxidation is not catalysed by the malic enzyme since it could be shown that in these extracts TPN is essential for malic enzyme activity, whereas no coenzyme requirement for anaerobic oxidation by ferricyanide could be demonstrated. Further, the marked inhibition of this oxidation by tartronic and maleic acids and the much lower Km value are not in agreement with the properties of the malic dehydrogenase of pig-heart extracts or resting suspensions of E8ch. coli. It seems most likely that the responsible enzyme is similar to malic dehydrogenase but with physical constants differing from those found for the enzyme obtained from other sources. A binding of coenzyme by the dehydrogenase similar to that of DPN by glyceraldehyde 3-phosphate dehydrogenase (Velick, Hayes & Harting, 1953) may occur, however, and thus obviate the need for additional coenzyme. This dehydrogenase is inhibited by me8otartaric, tartronic, maleic, malonic, i8ocitric and citric acids, and the inhibition by me8otartaric, tartronic and citric acids has been shown to be competitive. The K, values found are not in agreement with those reported for L-malic dehydrogenase or the malic enzyme of various origins.
In 2001 the University of New South Wales Faculty of Medicine embarked on designing a curriculum-management system to support the development and delivery of its new, fully integrated, outcome-based, six-year undergraduate medicine program. The Web-enabled curriculum-management system it developed is known as eMed, and it comprises a suite of integrated tools used for managing graduate outcomes, content, activities, and assessment in the new program. The six main tools are a curriculum map, timetable, student portfolio, peer feedback tool, assessment tracking, and results tools. The eMed functions were determined by organizational and curricular needs, and a business management perspective guided its development. The eMed project was developed by a multidisciplinary team, and its successful development was achieved mostly by methodically identifying the scope of each tool and the business processes it supports. Evaluation results indicated a high level of user acceptance and approval. The eMed system is a simple yet effective educational technology system that allows users to evaluate and improve the curriculum in real time. As a second-generation curriculum-management system, eMed is much more than an educational administration system; it is a knowledge network system used by staff and students to transform data and information into knowledge and action. The integration of learning and assessment activities data in the one system gives a depth of curriculum information that is unusual and that allows for data-based decision making. Technologically, eMed helps to keep the medicine program up to date. Organizationally, it strengthens the school's data-driven decision-making process and knowledge network culture.
On the basis of body weight, mice showed a higher percentage survival to large doses of insulin than did rabbits and these in turn were more resistant to insulin than guinea pigs. Antibodies to insulin were induced in five species of animals. Anti-insulins produced by the guinea pig, rabbit, sheep, and horse can each neutralize insulin extracted from the pancreas of the rabbit, sheep, horse, pig, ox, and monkey (Macacus rhesus), but none of the four can neutralize insulin extracted from guinea-pig pancreas. Guinea-pig anti-insulin can neutralize endogenous mouse insulin; horse anti-insulin cannot. The problem of the relative effectiveness of insulin as an antigen is discussed.
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