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Biomedical subjects

R L Miller

Publications and source records attributed to R L Miller.

At least 199 records · Page 11Linked to original sources
PubMed1982

Plasma pharmacokinetics of intravenously administered atropine in normal human subjects.

The pharmacokinetics of atropine (dl-hyoscyamine) was studied in six normal volunteers following a single 1-mg intravenous dose of atropine. Atropine plasma levels were collected for 24 hours and analyzed by radioimmunoassay. Pulse rates were monitored and compared with predose values in each subject. Atropine plasma concentrations were fitted by least-squares regression analysis. The observed maximal increase in pulse rate, at 12 to 16 minutes after the dose, correlated with the maximum predicted tissue levels of atropine based on the computer fit of the plasma atropine concentration-time data. No correlation between the time of maximum response and atropine plasma concentrations was observed. The average half-life of atropine was 4.125 hours. This data may be used to design a multiple-dosing regimen for intravenous atropine in patients.

Adult↗
PubMed1982

Purification, characterization, substrate and inhibitor specificity of adenosine kinase from several Eimeria species.

Ribonucleosides of some pyrazolo [3,4-d] pyrimidines have been shown to be potent anticoccidial agents. To investigate their interactions with adenosine kinase, this enzyme was purified by affinity chromatography from the sporulated oocysts of 3 avian coccidia, Eimeria tenella, E. acervulina and E. brunetti as well as from chicken liver. Comparative studies revealed several differences among the enzymes. Magnesium appeared not to be inhibitor of the E. tenella enzyme but did inhibit the enzymes from the other three sources. ATP in excess of the magnesium concentration strongly inhibited the E. brunetti enzyme but had only a small effect on the other enzymes. The chicken liver enzyme utilized a broader variety of triphosphate donors than did any of the enzymes from Eimeria species. ATP, dATP, GTP, dGTP and ITP was the best substrates. Studies with pyrazolo [3,4-d] pyrimidine nucleosides revealed two groups of enzymes with similar inhibitor specificities, the chicken liver and E. Acervulina vs. the E. tenella and E. brunetti enzyme. This grouping roughly correlates with the in vivo anticoccidial specificity of these compounds. Substrate specificity studies using two 4-substituted pyrazolo [3,4-d] pyrimidine ribonucleosides (ethylthio- and cinnamylthio-), which have shown potent anticoccidial activity in vivo, revealed that each served as a substrate for the enzymes from E. tenella and E. acervulina. The E. tenella enzyme was the more efficient at the phosphorylation of those compounds. However, only the ethylthio- compound was detectably phosphorylated by the enzyme from E. brunetti. In contrast to the inhibitor specificity, the substrate activities of these nucleosides do not correlate well with their in vivo anticoccidial activity.

Adenosine Kinase↗
PubMed1981

Subcutaneous phaeohyphomycosis caused by Exophiala moniliae.

The first documented case of phaeohyphomycosis in man caused by Exophiala moniliae is reported from South Australia. Study of herbarium specimens, living cultures, and other materials has revealed that E. moniliae was previously unknown in Australia.

Australia↗
PubMed1981

Secretin immunoreactivity in rat and pig brain.

Secretin immunoreactivity in rat and pig brain has been identified and characterized utilizing a highly specific radioimmunoassay and fractionation on a high pressure liquid chromatographic system reverse phase column. One immunoreactive peak from each brain extract was observed. Secretin immunoreactivity from rat brain and duodenum coelute, but eluted slightly ahead of the immunoreactivity from pig brain and duodenum and from synthetic porcine secretin. Immunoreactive secretin is widely distributed in the thalamus, hypothalamus and olfactory bulb, cerebral cortex, midbrain, septum, striatum, hippocampus, medulla and pons. The highest concentrations occur in the pineal and the pituitary gland.

Animals↗
PubMed1981

Release of alpha-melanocyte stimulating hormone into rat and human cerebrospinal fluid in vivo and from rat hypothalamus slices in vitro.

The release of alpha-melanocyte stimulating hormone (alpha-MSH) from central nervous system neurons was investigated and demonstrated in vivo and in vitro. alpha-MSH immunoreactivity in rat and human cerebrospinal fluid (CSF) is comprised of deacetylated alpha-MSH, alpha-MSH and the methionine sulfoxide forms of these peptides. The sulfoxides are formed artifactually upon extraction. alpha-MSH in rat CSF is unaffected by hypophysectomy but is markedly increased by electrical stimulation of the mesencephalic central gray. These data indicate that CSF alpha-MSH is primarily of neuronal origin, alpha-MSH is also released in a calcium dependent manner from hypothalamic slices in vitro. The fact that the release of alpha-MSH is stimulated by veratridine and inhibited by tetrodotoxin demonstrates the necessity for neuronal sodium influx for alpha-MSH release. The presence of an alpha-MSH neurosecretory process supports a neurotropic role for this peptide in the central nervous system.

Animals↗
PubMed1981

Evidence that N-acetylation regulates the behavioral activity of alpha-MSH in the rat and human central nervous system.

alpha-MSH immunoreactive peptides were fractionated and characterized in rat and human brain and rat pituitary by reversed phase high pressure liquid chromatographic techniques. alpha-MSH and deacetylated alpha-MSH were two major naturally existing peptides in both brain and pituitary gland. Subsequent experiments examined the roles of these two peptides in neuronal function. The alpha-MSH was clearly more effective than deacetylated alpha-MSH in improving performance on a visual discrimination task after intraperitoneal administration and in inducing excessive grooming after intraventricular administration. The difference in behavioral potency may be explained by the fact that alpha-MSH was much more resistant to peptidase degradation than was deacetylated alpha-MSH. N-acetylation of alpha-MSH may be an effective regulatory process for modulating the behavioral potency of the secretory product of alpha-MSH-containing pituitary cells and neurons.

Acetylation↗
PubMed1981

Identification, characterization, and distribution of secretin immunoreactivity in rat and pig brain.

Secretin immunoreactivity was detected in the central nervous system of the rat and pig with a highly specific radioimmunoassay. The secretin immunoreactivity in the rat and pig brain and duodenum extracts was fractionated by using a reverse-phase high-pressure liquid chromatographic system. The immunoreactive secretin from pig brain and duodenum coeluted precisely with synthetic porcine secretin. However, immunoreactive secretin extracted from rat brain and duodenum eluted slightly before porcine secretin. These data suggest a slight difference in the structure of rat and pig secretin. The detection of secretin in the brain lays the groundwork for studies to determine the role of the peptide in central nervous system function.

Animals↗
PubMed1981

A new radioimmunoassay for haloperidol: direct measurement of serum and striatal concentrations.

A sensitive and specific radioimmunoassay for haloperidol has been developed. Antibodies were elicited in rabbits immunized with haloperidol hemisuccinate coupled to bovine serum albumin. Optimum sensitivity was obtained with a 1:4000 dilution of the antisera, permitting the detection of as little as 2.6 ng/ml of haloperidol. Major metabolites of haloperidol did not cross-react in the assay. The method does not require an extraction procedure and can be performed using as little as a 5-microliter sample. Haloperidol levels in rat serum and striatum were determined with this method, after the i.v. administration of different dosages of the drug. The distribution and elimination of haloperidol was linear over the dose range to have an elimination half-life of approximately 2.6 hr at all three dosage levels.

Animals↗