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Biomedical subjects

C M King

Publications and source records attributed to C M King.

At least 163 records · Page 9Linked to original sources
PubMed1978

Revision and reorganization of a hospital pharmacy policy and procedure manual.

The development of a hospital pharmacy policy and procedure manual which can provide employees with an immediate source of current and reliable operating information is discussed. Flexibility and the capability to be readily revised were key factors in the design of the manual. A table of contents, a referencing system and physical specifications for the manual were determined. Policies and procedures on format, writing style, distribution, responsibility, revisions and additions, and review were established. Sample policies and procedures are presented. The concept of a procedure specialist to coordinate all activities regarding the manual was examined. It is recommended that all staff members participate in the development and revision of policies and procedures.

Manuals as Topic↗
PubMed1977

Administrative case study: analysis of a hospital pharmacy's manpower requirements.

Development of a method to determine the manpower requirements needed to adequately staff a pharmacy department in a 760-bed teaching hospital is discussed. The Michigan Hospital Staffing Methodology Manual, direct observations, interviews and diaries were used to gather data. An example of the data collected for the dispensing area is presented. The data provided a basis for developing productivity standards for current methods and procedures used in the pharmacy department. Also, the data facilitated the justification process for allocating existing and requesting future manpower resources.

Costs and Cost Analysis↗
PubMed1976

Comparative adduct formation of 4-aminobiphenyl and 2-aminofluorene derivatives with macromolecules of isolated liver parenchymal cells.

Isolated parenchymal cells of rat liver have been used in a study of the metabolic activation of derivatives of the carcinogens 4-aminobiphenyl and 2-aminofluorene. The formation of adducts of these compounds with cellular RNA and protein has been taken as evidence of their transformation to metabolites that are capable of spontaneous reaction with tissue macromolecules. The hydroxamic acid N-hydroxy-N-4-acetylaminobiphenyl was bound to RNA to a greater extent than were the amino-, hydroxylamino-, nitroso-, nitro-, acetylamino-, or azoxybiphenyl derivatives. RNA adducts of the hydroxamic acid retained little of the acetyl group. The structural requirements for binding and the nature of the bound derivatives are consistent with the activation of N-hydroxy-N-4-acetylaminobiphenyl by N leads to O acyltransfer. Approximately equal quantities of 4-nitrosobiphenyl and the hydroxamic acid were bound to protein, but far less of the nitroso derivative was incorporated into RNA. Adduct formation of N-hydroxy-N-2-acetylaminofluorene with RNA occurred with retention of the acetyl group and was dependent on the concentration of sulfate in the media. Consequently, reaction of the fluorenyl derivative with RNA probably resulted from conjugation of the hydroxamic acid with sulfate.

Acetates↗
PubMed1975

Evidence for a second arylhydroxamic acid acyltransferase species in the small intestine of the rat.

The small intestine of the Sprague-Dawley rat has been shown to contain two species of arylhydroxamic acid acyltransferases. These enzymes were separable by gel filtration on Sephadex G-100. The smaller species had the mobility of rat liver acyltransferase and was precipitated with antiserum directed against the liver enzyme. The larger species was not precipitated with this antiserum. These species differ in their relative abilities to utilize N-hydroxy-N-2-acetylaminofluorene (N-hydroxy-AAF) and N-hydroxy-N-4-acetylaminobiphenyl (N-hydroxy-AABP) as substrates, and in their inhibition by non immune serum.

Acetyltransferases↗
PubMed1975

Irradiation-induced adduct formation of RNA with carcinogenic arylamine derivatives.

Radiolysis of N2O-saturated solutions of transfer RNA (tRNA) and the arylacethydroxamic acids, N-hydroxy-N-2-acetylaminofluorene and N-hydroxy-N-4-acetylaminobiphenyl; their corresponding acetamides, 2-acetylaminofluorene and 4-acetylaminofluorene; or the O-glucuronide of N-hydroxy-N-2-acetylaminofluorene resulted in adduct formation of the nucleic acid with these carcinogenic arylamine derivatives. The yield of adducts on irradiation of the arylacethdroxamic acids with tRNA was greater than that for their corresponding acetamides or the O-glucuronide. The fluorenylacethydroxamic acid and acetamide were also more reactive than the biphenyl analogs. Adduct formation resulting from radiolysis of tRNA and the arylacethydroxamic acids or the O-glucuronide proceeded with retention of both the aromatic nucleus and the N-acetyl group. The yields of adducts were much greater for irradiated mixtures than for irradiation of either component alone followed by mixing. Evaluation of the data shows that initial modification of the tRNA or the carcinogen can lead to adduct formation. In the case of primary radical attack of the nucleic acid, it has been shown that short-lived reactive RNA intermediates are responsible for a major fraction of the observed yield of adducts in the irradiated mixtures. Comparative studies showed that irradiation under conditions that favor reaction of oxidizing radicals enhanced formation of the adducts. Oxygen was shown to protect RNA from irradiation-induced binding of the arylacethydroxamine acids due to competition of O2 with the carcinogen for the reactive RNA intermediates.

Aminobiphenyl Compounds↗
PubMed1975

Activation of carcinogenic arylhydroxamic acids by human tissues.

Incubation of the carcinogenic arylhydroxamic acids N-hydroxy-N-2-fluorenylacetamide or N-hydroxy-N-4-biphenylacetamide and tRNA with 105,000 times g supernatants of homogenates of human small intestine, liver, or colon led to formation of arylamine-substituted nucleic acid adducts. These data indicated that enzymes of human tissues could activate arylhydroxamic acids by N leads to O acyl transfer. The unstable N-acetoxyarylamines formed by these enzymes reacted spontaneously with the tRNA to give covalently linked adducts with the nucleic acid.

Acyltransferases↗
PubMed1975

Comparative effects of strain, species, and sex on the acyltransferase- and sulfotransferase-catalyzed activations of N-hydroxy-N-2-fluorenylacetamide.

The arylhydroxamic acid acyltransferase, an enzyme that promotes the introduction of arylamine groups into nucleic acids, is greater in the stomach, small intestine, colon, and lung of the Sprague-Dawley rat than in comparable tissues of Fischer animals. The enzyme is distributed relatively evenly from the glandular stomach to the distal portion of the colon. No consistent differences in acyltransferase activities of the liver, kidney, brain, or spleen of these two strains were noted. Acyltransferase activity was readily demonstrable in the livers of guinea pigs, hamsters, rabbits, and monkeys; in the kidneys of guinea pigs and hamsters; in the stomachs of guinea pigs and hamsters; in the small intestines of guinea pigs, hamsters, rabbits, and monkeys; in the colons of guinea pigs and hamsters; and in lungs of hamsters. Mouse, dog, and goat tissues were essentia-ly devoid of acyltransferase activity. The transformation of N-hydroxy-N-2-fluorenylacetamide into a reactive species by conjugation with sulfate was carried out with 105,000 times g supernatants of liver from Sprague-Dawley and Fischer rats and their Flhydrids. The abilities of liver extracts from the hybrids to carry out this activation were intermediate between those from animals of the same sex of the two parental strains.

Acetyltransferases↗
PubMed1968

Enzyme-catalyzed reactions of the carcinogen N-hydroxy-2-fluorenylacetamide with nucleic acid.

A protein fraction obtained by gel filtration of a 105,000g supernatant of rat liver catalyzes three reactions of the hepatocarcinogen N-hydroxy-2-fluorenylacetamide with nucleic acid. Cofactor requirements and isotopic studies suggest that the reactive intermediates involved may be N-2-fluorenylhydroxylamine, and phosphate and sulfate esters of N-hydroxy-2-fluorenylacetamide.

Adenosine Triphosphate↗