Biomedical subjects

M C Carson

Publications and source records attributed to M C Carson.

9 recordsLinked to original sources

PubMed2001

Kinematic analysis of a multi-segment foot model for research and clinical applications: a repeatability analysis.

An unbiased understanding of foot kinematics has been difficult to achieve due to the complexity of foot structure and motion. We have developed a protocol for evaluation of foot kinematics during barefoot walking based on a multi-segment foot model. Stereophotogrammetry was used to measure retroreflective markers on three segments of the foot plus the tibia. Repeatability was evaluated between-trial, between-day and between-tester using two subjects and two testers. Subtle patterns and ranges of motion between segments of the foot were consistently detected. We found that repeatability between different days or different testers is primarily subject to variability of marker placement more than inter-tester variability or skin movement. Differences between inter-segment angle curves primarily represent a shift in the absolute value of joint angles from one set of trials to another. In the hallux, variability was greater than desired due to vibration of the marker array used. The method permits objective foot measurement in gait analysis using skin-mounted markers. Quantitative and objective characterisation of the kinematics of the foot during activity is an important area of clinical and research evaluation. With this work we hope to have provided a firm basis for a common protocol for in vivo foot study.

Biomechanical Phenomena↗

PubMed2000

Ion-pair solid-phase extraction.

Solid-phase extraction (SPE) is a technique widely employed by analytical chemists. SPE cartridges are available in a wide variety of formats containing media with diverse chemistries. This paper will review ion-pair SPE, one of the less frequently applied, and presumably less well-known techniques. Advantages of this technique over more conventional reversed-phase or ion-exchange SPE include selectivity, compatibility with rapid evaporative concentration, and potential application to multiclass multiresidue analysis.

Chromatography, Ion Exchange↗

PubMed1999

Antibiotic residues in milk samples obtained from cows after treatment for papillomatous digital dermatitis.

OBJECTIVE: To determine whether there would be detectable antibiotic residues in milk obtained from dairy cattle with papillomatous digital dermatitis (PDD) after topical treatment with oxytetracycline. DESIGN: Randomized controlled clinical trial. ANIMALS: 28 lactating Holstein cows with PDD. PROCEDURE: Cows were assigned to 2 treatment groups. Treatment 1 (n = 16) consisted of spraying of PDD lesions with 15 ml of a solution containing 100 mg of oxytetracycline/ml; lesions were sprayed twice daily for 7 days, using a garden sprayer. Treatment 2 (n = 12) consisted of a one-time application of a bandage that consisted of cotton soaked with 20 ml of a solution containing 100 mg of oxytetracycline/ml. Milk samples were obtained before and after treatment and assayed for tetracycline content by use of high-performance liquid chromatography and a commercially available tetracycline screening test. RESULTS: None of the cows in either treatment group had violative residues of oxytetracycline in milk samples. CONCLUSIONS AND CLINICAL RELEVANCE: Producers treating lactating cows that have PDD, via topical application of oxytetracycline solution at the concentrations reported in this study, have a low risk of causing violative antibiotic residues in milk.

Animals↗

PubMed1998

Confirmation of spectinomycin in milk using ion-pair solid-phase extraction and liquid chromatography-electrospray ion trap mass spectrometry.

A confirmation procedure is described for residues of spectinomycin in bovine milk. Spectinomycin is extracted from raw milk using ion-pair reversed-phase solid-phase extraction. The extracts are ion-pair chromatographed on a polymeric reversed-phase column and analyzed on a quadrupole ion trap mass spectrometer equipped with an electrospray interface. MS-MS data are acquired in the scan mode of product ions deriving from m/z 333, the protonated molecular ion. The estimated limit of confirmation is between 0.05 and 0.1 microg/ml. The procedure was validated with control milk, fortified milk (0.1-5.0 microg/ml), and milk from cows dosed with spectinomycin.

Animals↗

PubMed1998

Confirmation of multiple tetracycline residues in milk and oxytetracycline in shrimp by liquid chromatography-particle beam mass spectrometry.

A confirmation procedure is described for detection of residues of six tetracyclines in bovine milk, and oxytetracycline in shrimp. Residues are extracted from milk or shrimp tissue using metal chelate affinity chromatography. The extracts are desalted, further concentrated using polymeric solid-phase extraction, and chromatographed on a polymeric reversed-phase column. Analysis is by methane negative ion chemical ionization on a quadrupole mass spectrometer using a particle beam interface. Data are acquired in partial scan mode, monitoring from m/z 378 to m/z 480. The procedure was validated with control milk and shrimp, fortified milk (30 ng/ml) and shrimp (100 ng/g), and milk and tissue from animals treated with the drugs.

Animals↗

PubMed1987

Angiotensin II receptors and mechanisms of action in adrenal glomerulosa cells.

The plasma-membrane receptors, coupling mechanisms, and effector enzymes that mediate target-cell activation by angiotensin II (AII) have been characterized in rat and bovine adrenal glomerulosa cells. The AII holoreceptor is a glycoprotein of Mr approximately 125,000 under non-denaturing conditions. Photoaffinity labeling of AII receptors with azido-AII derivatives has shown size heterogeneity among the AII binding sites between species and target tissues, with Mr values of 55,000 to 79,000. Such variations in molecular size probably reflect differences in carbohydrate content of the individual receptor sites. The adrenal AII receptor, like that in other tissues, is coupled to the inhibitory guanine nucleotide inhibitory protein (Ni). However, studies with pertussis toxin have shown that stimulation of aldosterone production by AII is not mediated by Ni but by a pertussis-insensitive nucleotide regulatory protein of unidentified nature. Although Ni is not involved in the stimulatory action of AII on steroidogenesis, it does mediate the inhibitory effects of high concentrations of AII upon aldosterone production. The actions of AII on adrenal cortical function are thus regulated by at least two guanine nucleotide regulatory proteins that are selectively activated by increasing AII concentrations. The principal effector enzyme in AII action is phospholipase C, which is rapidly stimulated in rat and bovine glomerulosa after AII receptor activation. AII-induced breakdown of phosphatidylinositol bisphosphate (PIP2) and phosphatidylinositol phosphate (PIP) leads to formation of inositol 1,4,5-trisphosphate (IP3) and inositol 1,4-bisphosphate (IP2). These are metabolized predominantly to inositol-4-monophosphate, which serves as a marker of polyphosphoinositide breakdown, whereas inositol-1-phosphate is largely derived from phosphatidylinositol hydrolysis. The AII-stimulated glomerulosa cell also produces inositol 1,3,4-trisphosphate, a biologically inactive IP3 isomer formed from Ins-1,4,5-trisphosphate via inositol tetrakisphosphate (IP4) during ligand activation in several calcium-dependent target cells. The Ins-1,4,5-P3 formed during AII action binds with high affinity to specific intracellular receptors that have been characterized in the bovine adrenal gland and other AII target tissues, and may represent the sites through which IP3 causes calcium mobilization during the initiation of cellular responses.

Adrenal Glands↗

PubMed1987

Physicochemical characterization of photoaffinity-labeled angiotensin II receptors.

Specific receptor sites for angiotensin II (AII) were analyzed in the adrenal cortex and other target tissues including liver, anterior pituitary gland, and smooth muscle, after covalent labeling with the radioactive photoaffinity analog 125I-[Sar1,(4-N3)Phe8]-AII. The photoreactive AII derivative retained high affinity for adrenal receptors and full steroidogenic activity in adrenal glomerulosa cells. In bovine adrenal cortex, covalent labeling of AII receptors by the photoreactive analog was specifically inhibited by [Sar1]AII with an IC50 of about 5 nM. The Mr of the covalent AII-receptor complex during polyacrylamide gel electrophoresis of the labeled protein under reducing conditions was 58,000. Under non-reducing conditions, a minor band with Mr of 105,000 was also observed. Two labeled species were also found during gel permeation chromatography of the detergent-solubilized complex, with Mrs of 64,000 and 86,000. The pl of the solubilized photolabeled complex was absorbed to wheat germ lectin Sepharose 6MB and could be eluted by N-acetylglucosamine. The Mrs of specific AII-binding sites in several target tissues, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, showed target tissues, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, showed significant differences within and between species. The most striking differences were between rat adrenal cortex (79,000) and both rat liver (60,000) and bovine adrenal cortex (58,000). After enzymatic deglycosylation, the Mr of the major component present in the bovine and rat adrenal cortex decreased by 40% and 55% to 35,000 and 34,000, respectively, suggesting that variations in carbohydrate content contribute to the physical heterogeneity of AII receptors in individual target tissues.

Adrenal Cortex↗

PubMedDate not supplied

Simultaneous determination of multiple tetracycline residues in milk using metal chelate affinity chromatography.

A method was developed for the determination of 7 tetracyclines in milk. Raw milk samples are defatted, acidified, and centrifuged to remove proteins, and the tetracyclines are specifically absorbed from the milk by chelation with metal ions bound to small Chelating Sepharose Fast Flow columns. The tetracyclines are removed from these columns with EDTA-containing buffer, and the extracts are further cleaned up by centrifugal ultrafiltration. Finally, the extracts are concentrated and analyzed simultaneously by on-line concentration. This method has limits of detection for individual tetracyclines of < 5 ng/mL and was validated with fortified milk samples at 15, 30, and 60 ng/mL. Recoveries exceeded 60% for all tetracyclines at all levels, with good precision. The method was also tested on milk from cows dosed with each of the tetracyclines. Advantages of this method over existing methods include its sensitivity, minimal use of organic solvents, and speed; with an autosampler, at least 14 samples can be processed and analyzed in 1 day.

Animals↗

PubMedDate not supplied

Simultaneous determination of multiple tetracycline residues in milk by metal chelate affinity chromatography: collaborative study.

To meet federal and state regulatory needs, a liquid chromatographic (LC) method with ultraviolet (UV) detection was developed for determination of 7 tetracyclines at 30 ng/ml in milk. Raw milk samples are defatted, acidified, and centrifuged to remove proteins, and tetracyclines are specifically absorbed from the milk by chelation with metal ions bound to small Chelating Sepharose Fast Flow columns. Tetracyclines are removed from these columns with EDTA-containing buffer, and extracts are further cleaned by ultrafiltration. Finally, extracts are concentrated and analyzed simultaneously by using on-line concentration. This method was validated in a collaborative study that involved 11 laboratories, including the authors' laboratory. Each laboratory was asked to prepare and analyze known control and fortified milk samples, as well as 18 coded blind samples. Eight laboratories completed all analyses. Average interlaboratory recoveries for the known fortified samples ranged from 59% (methacycline at 15 ng/ml) to 78% (oxytetracycline at 60 ng/ml). Average recovery for each of 7 residues at 30 ng/ml were between 60 and 110%, meeting single-residue guidelines for accuracy set by the U.S. Food and Drug Administration. Reproducibility relative standard deviation (RSDR) for the known fortified samples varied from 11 to 39%, with 6 of 7 residues at the 30 ng/ml level having RSDR values at or below 20%. Seven of 8 laboratories correctly identified blind control milk samples and all 28 residues present in blind samples. The metal chelate affinity-LC method for determination of multiple tetracycline residues in milk has been adopted first action by AOAC INTERNATIONAL.

Animals↗