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Biomedical subjects

M L Stewart

Publications and source records attributed to M L Stewart.

At least 37 records · Page 2Linked to original sources
PubMed1982

The metabolism of a series of methylalkylnitrosamines.

The microsomal metabolism of eight methyl alkyl nitrosamines (nitrosotrifluoroethylamine, nitrosomethylpropylamine, nitrosomethylpentylamine, nitrosomethylneopentylamine, nitrosomethylhexylamine, nitrosomethylheptylamine, nitrosomethylcyclohexylamine and nitrosomethylbenzylamine) was studied. All the nitrosamines produced formaldehyde during metabolism but only nitrosotrifluoroethylamine failed to produce the expected second carbonyl product. All the nitrosamines with the exception of nitrosomethylpropylamine exhibited simple Michaelis-Menten kinetics. The latter compound showed two distinct kinetic curves. The chain length of the second alkyl moiety appeared to have a profound influence on the metabolism of the methyl group to formaldehyde.

Animals↗
PubMed1982

Relationship between carcinogenicity and in vitro metabolism of nitrosomethylethylamine, nitrosomethyl-N-butylamine, and nitrosomethyl-(2-phenylethyl)amine labeled with deuterium in the methyl and alpha-methylene positions.

With the use of rat liver preparations, the in vitro microsomal metabolism of methylethylnitrosamine, methyl-n-butylnitrosamine, and methyl(2-phenylethyl)nitrosamine labeled with deuterium in the methyl and alpha-methylene positions has been compared with that of the parent (unlabeled) compounds. All three forms of the liver carcinogen methylethylnitrosamine are metabolized with two sets of kinetic constants. Examination of these kinetic constants suggests that both methylation and ethylation of cellular nucleophiles might be important in the carcinogenic action of these nitrosamines. The esophageal carcinogen, methyl(2-phenylethyl)nitrosamine, gave only one set of kinetic constants during metabolism. The metabolism of the three methylbutylnitrosamines gave results similar to that of the three methylethyl nitrosamines. Except for metabolism of d2-methylbutylnitrosamine to butyraldehyde, two sets of kinetic constants were found. Approximately equivalent amounts of methylating species were produced from d3-methylbutylnitrosamine and d0-methylbutylnitrosamine.

Animals↗
PubMed1980

Mechanism(s) of altered mitochondrial calcium transport in acutely ischemic canine hearts.

Studies were undertaken to determine the mechanisms leading to altered mitochondrial function in ischemic myocardium. A new procedure has been developed to routinely isolate 60-70% of the total mitochondrial protein from heart tissue. After 1 hour of ischemia, mitochondria exhibit decreases of more than 50% in phosphorylating respiration for both NADH- and succinate-linked substrates compared to controls. However, no significant decreases in the efficiency of mitochondrial ATP synthesis (ADP:0) or ATPase activity are observed. Rates of substrate-driven Ca2+ uptake exhibit decreases greater than that seen with phosphorylating respiration with incomplete uptake and premature release of Ca2+. Spectrophotometric measurements in ischemic heart reveal rapid oxidation or loss of mitochondrial NADH with marked "swelling" of the inner membrane compartment; both changes parallel the loss of Ca2+. Significant losses in intramitochondrial adenine nucleotides also are found. Mitochondrial retention of accumulated Ca2+ can be restored by addition of small amounts of exogenous adenine nucleotides (ATP or ADP) with concomitant attenuation of both NADH oxidation and "swelling." The data indicate that, following 1 hour of ischemia, the efficiency of mitochondrial ATP production is still relatively intact whereas both electron transport chain activity and calcium transport are severely compromised. These decreases appear to be related to selective membrane damage in the mitochondrial inner membrane.

Acute Disease↗
PubMed1973

Purification of oncornaviruses by agglutination with concanacalin A (murine leukemia virus-phytohemagglutinin-friend virus).

Concanavalin A (Con A) has been used to rapidly and selectively agglutinate murine and avian oncornavirions from culture medium or plasma. The agglutinated virus was concentrated rapidly and gently by low-speed centrifugation and solubilization with alpha-methyl mannoside. Infectious virus was purified 2.3 times with respect to nucleic-acid content, and more than 60% of its infectivity was recovered. Infectious particles of densities 1.18 and 1.16 g/cm(3) were found in mouse cells infected with Friend virus. Con A reacted only with particles of density 1.16 g/cm(3), indicating heterogeneity with respect to carbohydrate content or structure as well as buoyant density. Electron microscopy of virus agglutinated with Con A showed a zone of Con A-glycoprotein complexes averaging 12-15 nm in thickness.

Agglutination↗
PubMed1971

Aurintricarboxylic acid: inhibitor of initiation of protein synthesis.

Aurintricarboxylic acid prevents the attachment of bacteriophage messenger RNA to ribosomes. As a consequence, initiation of protein synthesis in cell-free extracts prepared from Escherichia coli or rabbit reticulocytes is inhibited at concentrations of dye that do not prevent chain extension. Its properties can be distinguished from other agents that inhibit protein synthesis, including sodium fluoride, cycloheximide, and pactamycin.

Animals↗