Novel inhibition of carbonic anhydrase isozymes I, II and III by carbamoyl phosphate

Carbamoyl phosphate has been shown to inhibit carbonic anhydrase (CA) isozymes CA I, CA II and CA III. This physiologically important molecule is the most potent, naturally occurring inhibitor of carbonic anhydrase yet found. It is also unique, among carbonic anhydrase inhibitors discovered hitherto, in that it inhibits the 3 isozymes with equal effect, despite their strikingly different properties. The results imply the participation of carbonic anhydrase in the regulation of substrate availability for the urea cycle.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/24933/1/0000360.pd

Aerobic and anaerobic energy expenditure during rest and activity in montane Bufo b. boreas and Rana pipiens

The relations of standard and active aerobic and anaerobic metabolism and heart rate to body temperature ( T b ) were measured in montane groups of Bufo b. boreas and Rana pipiens maintained under field conditions. These amphibians experience daily variation of T b over 30°C and 23°C, respectively (Carey, 1978). Standard and active aerobic and anaerobic metabolism, heart rate, aerobic and anaerobic scope are markedly temperature-dependent with no broad plateaus of thermal independence. Heart rate increments provide little augmentation of oxygen transport during activity; increased extraction of oxygen from the blood probably contributes importantly to oxygen supply during activity. Development of extensive aerobic capacities in Bufo may be related to aggressive behavior of males during breeding. Standard metabolic rates of both species are more thermally dependent than comparable values for lowland relatives. Thermal sensitivity of physiological functions may have distinct advantages over thermally compensated rates in the short growing season and daily thermal fluctuations of the montane environment.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47726/1/442_2004_Article_BF00348070.pd

Mouse Chromosome 3

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/46995/1/335_2004_Article_BF00648421.pd

Carbonic Anhydrase II Deficiency in 12 Families with the Autosomal Recessive Syndrome of Osteopetrosis with Renal Tubular Acidosis and Cerebral Calcification

Osteopetrosis with renal tubular acidosis and cerebral calcification was identified as a recessively inherited syndrome in 1972. In 1983, we reported a deficiency of carbonic anhydrase II, one of the isozymes of carbonic anhydrase, in three sisters with this disorder. We now describe our study of 18 similarly affected patients with this syndrome in 11 unrelated families of different geographic and ethnic origins. Virtual absence of the carbonic anhydrase II peak on high-performance liquid chromatography, of the esterase and carbon dioxide hydratase activities of carbonic anhydrase II, and of immunoprecipitable isozyme II was demonstrated on extracts of erythrocyte hemolysates from all patients studied. Reduced levels of isozyme II were found in obligate heterozygotes. These observations demonstrate the generality of the findings that we reported earlier in one family and provide further evidence that a deficiency of carbonic anhydrase II is the enzymatic basis for the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification. We also summarize the clinical findings in these families, propose mechanisms by which a deficiency of carbonic anhydrase II could produce this metabolic disorder of bone, kidney, and brain, and discuss the clinical evidence for genetic heterogeneity in patients from different kindreds with this inborn error of metabolism. (N Engl J Med 1985; 313:139–45.). © 1985, Massachusetts Medical Society. All rights reserved.SCOPUS: ar.jinfo:eu-repo/semantics/publishe