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Biomedical subjects

A C Peacock

Publications and source records attributed to A C Peacock.

At least 19 recordsLinked to original sources
PubMed2005

Exact solutions of the generalized nonlinear Schrödinger equation with distributed coefficients.

A broad class of exact self-similar solutions to the nonlinear Schrödinger equation (NLSE) with distributed dispersion, nonlinearity, and gain or loss has been found describing both periodic and solitary waves. Appropriate solitary wave solutions applying to propagation in optical fibers and optical fiber amplifiers with these distributed parameters have also been studied in detail. These solutions exist for physically realistic dispersion and nonlinearity profiles. They correspond either to compressing or spreading solitary pulses which maintain a linear chirp or to chirped oscillatory solutions. The stability of these solutions has been confirmed by numerical simulations of the NLSE with perturbed initial conditions. These self-similar propagation regimes are expected to find practical application in both optical fiber amplifier systems and in fiber compressors.

Journal Article↗
PubMed2003

Exact self-similar solutions of the generalized nonlinear Schrödinger equation with distributed coefficients.

A broad class of exact self-similar solutions to the nonlinear Schrödinger equation (NLSE) with distributed dispersion, nonlinearity, and gain or loss has been found. Appropriate solitary wave solutions applying to propagation in optical fibers and optical fiber amplifiers with these distributed parameters have also been studied. These solutions exist for physically realistic dispersion and nonlinearity profiles in a fiber with anomalous group velocity dispersion. They correspond either to compressing or spreading solitary pulses which maintain a linear chirp or to chirped oscillatory solutions. The stability of these solutions has been confirmed by numerical simulations of the NLSE.

Journal Article↗
PubMed1985

Two-dimensional electrophoretic display of restriction fragments from genomic DNA.

We have developed a procedure for the resolution of restriction enzyme digests of mammalian genomic DNA in two dimensions. Fragments from a first digestion are separated on a column of purified agarose containing a second restriction enzyme in the absence of the divalent cation required for enzyme activity. After enzyme activation and digestion, the fragments are resolved on an agarose slab gel. We have digested rat genomic DNA and found in the ethidium-stained pattern a variety of features which have not been described previously.

Animals↗
PubMed1985

Prolactin homogeneously induces the tRNA population of mouse mammary explants.

Explants of mouse mammary glands were cultured with and without prolactin in the presence of inorganic [32P] to estimate the effect of prolactin on tRNA synthesis. Labeled tRNA was extracted and characterized by two-dimensional gel electrophoresis. tRNA synthesis was 2-3 fold greater in the presence of prolactin; and the synthesis rate of each resolvable tRNA species was increased proportionally. tRNA populations from mouse mammary tissues at three stages of development were also examined. Alterations were noted between early pregnant and fully lactating tissues. The results of this study provide evidence that the tRNA population, which is known to be "specialized" for casein synthesis in the mammary gland, is determined as the gland develops and prepares for lactation.

Animals↗
PubMed1984

Occupational therapists: personality and job performance.

This study was conducted to determine the personality structure of a group of occupational therapists and to examine the relationship between specific personality variables and job performance of practicing occupational therapists. The results indicated that occupational therapists as a group are not distinguishable from people in general, in terms of personality; however, a number of personality variables were significantly related to job performance. Implications for both the field of occupational therapy and for the selection of students are discussed.

Employee Performance Appraisal↗
PubMed1981

Haptoglobin and albumin synthesis in isolated rat hepatocytes. Response to potential mediators of the acute-phase reaction.

Incorporation of [3H]leucine into haptoglobin and albumin by isolated rat hepatocyte suspensions was studied to assess the role of potential mediators of the acute-phase reaction in promoting haptoglobin synthesis. In vitro, in the presence of insulin, the addition of a hormone mixture containing hydrocortisone, glucagon, somatotropin, and triiodothyronine resulted in a 70% increase in leucine incorporation into haptoglobin relative to albumin at 48 h incubation. A variety of agents, selected because they are considered to play some part in the acute-phase reaction, were added to the medium, and similar measurements of leucine incorporation were made. The specific binding to hepatocytes by asialo- and asialo, agalacto-derivatives of haptoglobin or orosomucoid did not affect synthesis of haptoglobin or albumin. Epinephrine, prostaglandins E1 and E2, bacterial lipopolysaccharide, and sera containing active complement components also failed to stimulate relative haptoglobin synthesis. A partially purified preparation of human leukocytic pyrogen, however, caused a 70% increase in leucine incorporation into haptoglobin relative to albumin in the present of the hormone mixture, suggesting that this substance may affect acute-phase protein synthesis.

Albumins↗
PubMed1980

The induction of liver microsomal proteins by 3-methylcholanthrene in rats of different age, sex and strain.

The treatment of male and female adult and male and female immature rats with 3-methylcholanthrene results in increases in the intensity of two liver microsomal protein bands separated by sodium dodecyl sulphate-polyacrylacrylamide gel electrophoresis. The induced protein species have estimated molecular weights of about 55 000 and 52 500. The time course of the induction of these species has been followed in a semi-quantitative manner. In immature rats an additional band, corresponding to a protein species with a molecular weight of about 43 000, is also increased by 3- methylcholanthrene treatment. In male adult rats exclusively, treatment with 3-methylcholanthrene also results in a decrease in the intensity of a band corresponding to a protein species of about 51 000. The appearance of this band in the liver microsomal fraction of adult male rats occurs following sexual maturation and its presence represents a significant difference in the microsomal proteins between male and female rats; this protein is not detected in younger rats or in female rats at any age. These findings are discussed in terms of their possible relevance to the cytochrome P-450 content of the endoplasmic reticulum of rat hepatocytes.

Animals↗
PubMed1977

Conformational states of 18 S rRNA from HeLa cells detected by gel electrophoresis.

Gel electrophoretic analysis has been used to study some of the conformational properties of 18 S rRNA from HeLa cells. After isolation and treatment by heat or denaturants, the mobility of the RNA in 3% acrylamide/0.5% agarose composite gels was found to be altered; often there were two or more distinct components. Several of these forms could be interconverted by heating to 40 degrees C or by use of dimethyl sulfoxide. Although these comformers were easily distinguishable (by their electrophoretic properties), their melting profiles were very similar. Only a single electrophoretic form was detected when electrophoresis was performed at 40 degrees C. The conformational differences observed are probably derived by variations in base pairing and stacking that result when the parent form is cooled.

Electrophoresis, Polyacrylamide Gel↗
PubMed1977

Bioassay for prolactin: densitometric analysis on polyacrylamide gels of milk protein production by mammary explants in vitro.

Mammary explants from mice in midpregnancy cultured in a synthetic medium containing insulin and hydrocortisone respond to the addition of prolactin by the synthesis of milk proteins. The secretory response in alveolar lumina has served as a histologic endpoint in a sensitive bioassay for prolactin developed by Kleinberg and Frantz (J Clin Invest 50: 1557, 1971). This report demonstrates that the quantitative densitometric analysis of stained milk proteins (caseins) made in response to prolactin is a useful modification of that bioassay. Electrophoretic analysis of the proteins extracted from the explants permits a quantitative estimate of casein content. The amount of casein present after 5 days of incubation was found to be a measure of the prolactin concentration in the medium. No radioactive isotopes are used. The use of electrophoretic analysis has practical advantages over the histologic scoring used earlier, and has approximately the same range of sensitivity.

Animals↗
PubMed1976

Determination of the subunit composition of haptoglobin 2-1 polymers using quantitative densitometry of polyacrylamide gels.

Human haptoglobin (Hp), a hemoglobin-binding glycoprotein containing two types of polypeptide chains, alpha and beta, in equimolar amounts linked by disulfide bonds, exists in three major phenotypes determined by the properties of the alpha chain: Hp 1-1 (alpha1), Hp 2-2 (alpha2), and Hp 2-1 (alpha1 and alpha2). Hp 2-2 and Hp 2-1 form a series of alpha-disulfide-linked polymers. The subunit composition of the Hp 2-1 series was studied by isolation of single Hp 2-1 polymers by polyacrylamide gel electrophoresis. After reductive disulfide cleavage and alkylation the relative content of alpha2 and alpha1 polypeptide chains was determined by quantitative densitometry of acid/urea polyacrylamide gels stained with Coomassie brilliant blue R250. The molar ratios alpha2/alpha1 for the Hp 2-1 polymers. P1 through P5 (in order of decreasing electrophoretic mobility), were found to be: P1, 0.0 (alpha1 only); P2, 0.48; P3, 0.97; P4, 1.6; P5, 2.0. Since one alphabeta-Hb half-molecule is known to bind to each Hp beta chain, the beta polypeptide chain content of each of the Hp 2-1 polymers could be estimated by by counting the number of Coomassie blue bands formed after electrophoresis of isolated Hp 2-1 polymers fractionally saturated with cyanmethemoglobin (Hb). The number of beta chains present in Hp 2-1 polymers P1 through P4 was determined to be: P1, 2; P2, 3; P3, 4 and P4, 5. Molecular weights of the Hp 2-1 polymers were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresus using as standards the almost homologous Hp 2-2 polymer series whose molecular weights are known from ultracentrifugation studies. Molecular weights for the first five Hp 2-1 polymers were estimated to be 107,000; 162,000; 217,000, 274,000; and 331,000, respectively. These data are consistent with the previously proposed model for the subunit composition of the Hp 2-1 polymer series when P1 = (alpha1 beta)2 and the subsequent polymers in order are represented as (alpha1 beta)2(alpha2 beta)n where n = 1,2,3,4...

Densitometry↗
PubMed1975

Hemoglobin binding by isolated polymeric proteins from human haptoglobin types 2-1 and 2-2. Some suggested polymer subunit compositions.

1. Some of the individual members of the polymeric series of proteins from human haptoglobin types 2-1 and 2-2 were isolated by gel electrophoresis. By reacting this purified material with less than an equivalent amount of hemoglobin and analyzing the result by electrophoresis, the number of haptoglobin-hemoglobin complexes could be clearly counted. For the haptoglobin 2-1 series, the number of complexes formed was n+1, where n is the serial order, in decreasing electrophoretic mobility, of the haptoglobin polymeric form used. For the haptoglobin 2-2 series, the number of complexes was n+2. 2. For the first three members of haptoglobin 2-1 series, the haptoglobin-hemoglobin composition of the complexes was estimated from scans of the unstained gels. The data indicated that this series consists of 2,3,4... alpha beta haptoglobin subunits, each of which can combine with an alpha beta subunit of hemoglobin.

Electrophoresis, Polyacrylamide Gel↗