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Biomedical subjects

C Ellis

Publications and source records attributed to C Ellis.

At least 127 records · Page 7Linked to original sources

Evaluation of an inhibitor assay to determine serum isoamylase distribution.

We tested a technique to distinguish salivary from pancreatic isoamylase using a wheat protein which inhibits salivary isoamylase. The inhibitor technique accurately reflected the preponderance of pancreatic or salivary isoamylase in sera which had been "spiked" with human pancreatic or salivary isoamylase. Comparison of the results of either cellulose acetate electrophoresis or isoelectric focusing showed an excellent correlation (r = 0.99) in 43 hyperamylasemic sera which did not contain macroamylase. Normal values obtained in 160 healthy subjects indicated that pancreatic isoamylase comprised 41 +/- 21% (1 SD) of total serum amylase activity and the upper limit of normal for serum pancreatic isoamylase was 166 IU/liter. The inhibitor assay provides a simple and accurate means of differentiating salivary from pancreatic hyperamylasemia.

Amylases↗

A rapid and simple assay to determine if macroamylase is the cause of hyperamylasemia.

Macromolecules are known to precipitate selectively in concentrated solutions of polyethylene glycol. This report describes the use of polyethylene glycol 6000 to distinguish macroamylase from normal-sized serum amylase. Preliminary studies indicated that a PEG concentration of 12% and a 10-min incubation at 37 degrees C separated normal serum amylase from macroamylase. Using these conditions, study of 18 macroamylase-containing sera showed precipitation of at least 73% of the amylase activity. In contrast, in 46 normal sera and 16 hyperamylasemic (but not macroamylasemic) sera, less than 52% of the amylase activity was precipitated by polyethylene glycol. This test provides a rapid, simple, and accurate means of determining if macroamylasemia is the cause of hyperamylasemia.

Amylases↗

Detection of intrauterine growth retardation by ultrasound: preliminary communication.

In this study, ultrasonic measurements of the fetal head area and abdominal area were obtained in 1200 patients with singleton pregnancies. The results from the 434 who have delivered, indicate that a large proportion of growth-retarded infants cannot be identified by a single late ultrasonic measurement of either area, at 32-34 weeks gestation, as has been previously suggested.

Abdomen↗

Reverse transcriptase from avian myeloblastosis virus.

From lots of 20 to 30 g of avian myeloblastosis virus RNA-dependent DNA polymerase was obtained in preparations of purity greater than 95% by using a two-step column chromatographic procedure employing DEAE (DE 52) and carboxymethylcellulose (CM 52.). Yields of RNA-dependent DNA polymerase varied from approximately 20,000 to 35,000 U/g of virus. Specific activity of the enzyme was about 35,000 to 60,000 U/mg of protein. Free of detectable RNase activity, the product exhibited a molecular weight of about 160,000, an isoelectric point of 6.5, and approximately 2 mol of fatty acid per mol of enzyme.

Animals↗

Bile acid metabolism in the cirrhotic rat.

Bile acid metabolism was studied in rats with cirrhosis induced by carbon tetrachloride (CCl4). Although the typical histologic features of cirrhosis were seen, cholestasis was not present in these animals as evidenced by a normal total serum bilirubin concentration and by a normal hepatic capacity to remove taurocholate infused intravenously. The cirrhotic rats also secreted taurocholate into bile at a normal rate. The total bile salt pool size in the cirrhotic rats was not significantly different from the pool size in normal rats (10.59 +/- 1.19 mumoles per gm. of liver (+/- 1 standard error of the mean) and 10.43 +/- 0.92 mumoles per gm. of liver, respectively). When the bile was drained externally through a chronic bile fistula, the normal rats increased the bile salt synthetic rate approximately 3-fold after 48 hours of drainage. However, the cirrhotic rats failed to significantly increase the synthetic rate for bile salts in response to biliary drainage. The normal rats also had a significant increase in cholic acid synthesis at the maximal synthetic rate, whereas the cirrhotic rats did not. These findings indicate that (when feedback inhibition is removed) CCl4 cirrhotic rats lack the ability to normally increase the activity of 7 alpha-hydroxylase and 12 alpha-hydroxylase, rate-limiting enzymes in the synthesis of bile salts.

Animals↗

Serum isoamylase measurements in pancreatitis complicating chronic renal failure.

This investigation was designed to determine whether serum isoamylase measurements can aid in establishing the diagnosis of acute pancreatitis in renal failure patients. Twenty-two hemodialysis patients were studied, four of whom had documented acute pancreatitis. Total serum amylase and pancreatic isoamylase concentrations were significantly higher (p less than 0.02) in the pancreatitis patients than in the 18 patients without pancreatitis, but there was appreciable overlap between these two groups. In each of the four patients with pancreatitis, the percentage of serum amylase derived from the pancreas (range, 80% to 90%) was well above the highest value (67%) observed in the patients without pancreatitis. These results suggest that determination of the percentage of serum amylase represented by pancreatic isoamylase is of assistance in establishing the diagnosis of acute pancreatitis in renal failure patients.

Acute Disease↗

Protein kinase from avian myeloblastosis virus.

A protein kinase associated with purified virions of avian myeloblastosis BAI strain A was partially purified by ion-exchange chromatography and gel filtration. The transfer of phosphate catalyzed by this enzyme required a divalent metal ion and ATP as phosphate donor. GTP could not be substituted for ATP, and the reaction was unaffected by either cyclic AMP or beef-heart protein-kinase inhibitor. Of the virus and nonvirus proteins tested as phosphate acceptors, only acidic proteins were phosphorylated. In particular, purified preparations of reverse transcriptase from avian myeloblastosis virus did not accept phosphate. The enzyme is a basic protein (pI = 9.3), and, on the basis of molecular sieving through Sephadex G-200 and velocity sedimentation on glycerol gradient, the protein kinase has a molecular weight of 45,000.

Adenosine Triphosphate↗