Wound management and infection control after trauma: implication for the intensive care setting.
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Accidents, Traffic↗
Biomedical subjects
M T Martin
Publications and source records attributed to M T Martin.
Electronic spectroscopy of cobalt angiotensin converting enzyme and its inhibitor complexes.
Zinc, the catalytically essential metal of angiotensin converting enzyme (ACE), has been replaced by cobalt(II) to give an active, chromophoric enzyme that is spectroscopically responsive to inhibitor binding. Visible absorption spectroscopy and magnetic circular dichroic spectropolarimetry have been used to characterize the catalytic metal binding site in both the cobalt enzyme and in several enzyme-inhibitor complexes. The visible absorption spectrum of cobalt ACE exhibits a single broad maximum (525 nm) of relatively low absorptivity (epsilon = 75 M-1 cm-1). In contrast, the spectra of enzyme-inhibitor complexes display more clearly defined maxima at longer wavelengths (525-637 nm) and of markedly higher absorptivities (130-560 M-1 cm-1). The large spectral response indicates that changes in the cobalt ion coordination sphere occur on inhibitor binding. Magnetic circular dichroic spectropolarimetry has shown that the metal coordination geometry in the inhibitor complexes is tetrahedral and of higher symmetry than in cobalt ACE alone. The presence of sulfur----cobalt charge-transfer bands in both the visible absorption and magnetic circular dichroic spectra of the cobalt ACE-Captopril complex confirm direct ligation of the thiol group of the inhibitor to the active-site metal.
Angiotensin-Converting Enzyme Inhibitors↗
Participation of the lone tryptophan residue of rat alpha-foetoprotein in its drug-binding sites. Comparison with rat serum albumin.
The participation in drug binding of the lone tryptophan residue of rat alpha-foetoprotein (alpha-FP) and serum albumin, the two main transport proteins of foetal serum, has been studied by two different techniques. Firstly, the effect on phenylbutazone and warfarin binding of the chemical derivatization of the lone tryptophan residue of both proteins by 2-nitrophenylsulphonyl chloride (NPS) was studied. Secondly, the effect of phenylbutazone binding on the intrinsic fluorescence of the tryptophan residue of rat alpha-FP and albumin was investigated. The specific modification of the proteins by NPS did not affect the binding of warfarin by rat alpha-FP and albumin, but greatly decreased the affinity of the high-affinity sites of rat alpha-FP for phenylbutazone, though the numbers of these sites were not significantly changed. However, for albumin a similar decrease in the affinity constant appeared to be due to the reaction conditions. The spectrofluorimetric studies showed that the lone tryptophan residue of alpha-FP and albumin was quenched by phenylbutazone binding, and the quenching paralleled the fractional saturation of the high-affinity site only in the case of albumin. The effect of phenylbutazone binding on the intrinsic fluorescence of rat alpha-FP indicated that the lone tryptophan residue of this foetal protein is not in the same molecular environment as that of albumin, not participating directly in the high-affinity site for phenylbutazone, and the effect may be via some induced conformational change in rat alpha-FP. These results also confirm our previous suggestion that the high-affinity sites for phenylbutazone and warfarin are different on the rat alpha-FP molecule. The results seem to indicate that this is also the case for albumin, but confirmation is necessary.
Animals↗
Adduct formation between soluble fibrin monomers and elastin.
Monomers of fibrin generated from fibrinogen by thrombin reacted with elastin to give a new addition product or adduct. The adduct formation results from a covalent bond between both proteins, formation of which is dependent on elastin, fibrinogen and Ca2+ concentrations; but, Factor XIIIa did not intervene. Addition of fibronectin, together with fibrinogen, as cold insoluble proteins from human plasma, and of soluble collagen from rat tail tendon did not inhibit the first reaction. This enabled us to elaborate a new artificial connective matrix.
Animals↗
Drug-binding properties of rat alpha-foetoprotein. Specificities of the phenylbutazone-binding and warfarin-binding sites.
Rat alpha-foetoprotein (alpha-FP) strongly binds the drugs warfarin and phenylbutazone, as does albumin; however, the binding sites for the two drugs seemed to be different. This possibility and the specificity of this/these drug-binding site(s) of rat alpha-FP were investigated by competitive protein-binding experiments with a variety of drugs, representing different pharmacological groups, and biomolecules that are strongly bound by the foetal protein and that are suspected to play a specific role during foetal development. The binding mechanisms were further investigated by using comparisons between computer-derived theoretical displacement curves and experimental points in order to distinguish different possible binding models. The results indicate: that warfarin and phenylbutazone are bound at two distinct sites on rat alpha-FP and that a negative modulatory effect is exerted between the two sites; that the degree of specificity of these two drug-binding sites is different, since the warfarin-binding site appears to be specific for the binding of coumarinic and anthranilic drugs whereas that for phenylbutazone is able to bind substances of very varied chemical structure and is more hydrophobic; that the phenylbutazone-binding site is the site that binds oestrogens that thyroid hormones and, probably, fatty acids and bilirubin are bound at (an)other site(s) but exert negative modulatory effects on phenylbutazone binding. The nature of the different binding areas of rat alpha-FP is compared with that of those already proposed for albumin. The potential risks of toxicity of such interactions between drugs and/or biomolecules on foetal development are also discussed.
Animals↗
Induction of murine T cell lymphoma expressing specific cytotoxic activity.
The present work reports the establishment of an antigen-specific cytotoxic T cell lymphoma line after immortalization with a murine leukemia virus. Lymph node cells from mice bearing a transplanted syngeneic MCA sarcoma were infected in vitro with radiation leukemia virus and injected intrathymically into cogeneic recipient mice. Some lymphomas of donor origin were established as permanent continuous cell lines in vitro. One of them, NS8, expressed Thy-1.2, Lyt-1, Lyt-2 and peanut agglutinin surface markers. These cells were cytotoxic in vitro for the tumor cell line corresponding to the immunizing MCA sarcoma. No significant cytolytic activities against other syngeneic or allogeneic sarcomas or lymphomas, nor against the mastocytoma P815 were observed. After several months of in vitro propagation, the specificity of the cytotoxic activity had degraded and the level of Lyt-2 or peanut agglutinin receptors dropped. These characteristics were restored with a single in vivo passage. Thus, murine leukemia virus can be used to immortalize antigen-specific cytotoxic T cells.
Animals↗
Low molecular weight copper-binding ligands in human bile.
The aim of this study was to detect and identify major low molecular weight (less than 10,000) copper-binding ligands in human bile. Modified gel chromatography was used as the method of ligand detection because it ensures the detection of labile as well as inert metal-ligand complexes. Conjugated bilirubin, peptides, and amino acids, primarily glycine, were isolated as the major ligands. In contrast to the other copper-binding ligands, the peptides were poor zinc binders, suggesting the possibility that they may confer necessary specificity to trace metal elimination.
Amino Acids↗
Pharmacokinetics of sodium amoxicillin in foals after intramuscular administration.
Pharmacokinetic values of sodium amoxicillin (22 mg/kg of body weight) in foals were determined after a single IM injection in 6 Quarter Horse foals at 3, 10, and 30 days of age. Serum amoxicillin concentrations were measured serially over a 24-hour period. The absorption of amoxicillin was rapid and followed a 1st-order elimination. Mean peak serum concentrations occurred 30 minutes after the injection in foals at all ages and were 17.31 +/- 9.59 micrograms/ml when the foals were 3 days old, 23.28 +/- 9.86 micrograms/ml when the foals were 10 days old, and 21.35 +/- 6.39 micrograms/ml when the foals were 30 days old. Serum samples collected beyond 8 hours after administration contained amoxicillin concentrations less than 0.05 micrograms/ml. The elimination rate constant increased with increasing age (0.5265 +/- 0.0891 hour-1 when the foals were 3 days old, 0.6494 +/- 0.1114 hour-1 when the foals were 10 days old, and 0.7112 +/- 0.1016 hour-1 when the foals were 30 days old). Serum clearance increased with increasing age (498.4 +/- 82.6 ml/hr/kg at 3 days, 631.6 +/- 170.5 ml/hr/kg at 10 days, and 691.2 +/- 127.3 ml/hr/kg at 30 days). Serum half-life decreased with increasing age (1.34 +/-0.243 hour at 3 days, 1.10 +/- 0.239 hour at 10 days, and 0.991 +/- 0.139 hour at 30 days), whereas the extrapolated concentration at time zero and apparent volume of distribution did not change during the first 30 days of age.
Amoxicillin↗
[Specific cytotoxic activity of a virus-induced murine lymphoma].
The NS8 lymphoma induced with Radiation Leukemia Virus (RadLV) presents in vitro a specific cytotoxic activity. This line was established from a lymphoma induced by injection of lymph node cells from mice bearing the MCA-fibrosarcoma T2 to congenic mice. These cells present a cytotoxic activity limited to the T2 cells. They develop no significant cytotoxic activity against other syngeneic or allogeneic tumoral lines.
Animals↗
Drug-binding properties of rat alpha 1-foetoprotein. Binding of warfarin, phenylbutazone, azapropazone, diazepam, digitoxin and cholic acid.
As part of an investigation into whether alpha 1-foetoprotein (alpha 1-FP) plays the same transport role in foetal serum as albumin does in the adult, the binding properties of both proteins were compared with respect to the binding of a series of compounds known to be bound by albumin's specific drug-binding sites. The binding of warfarin, phenylbutazone, azapropazone, diazepam, digitoxin and cholic acid by rat alpha 1-FP and serum albumin was studied by equilibrium dialysis at 4 degrees C. Rat alpha 1-FP was shown to have neither albumin's high-affinity site II (diazepam as marker) nor its site III (digitoxin and cholic acid as markers). High-affinity binding by alpha 1-FP was found for the specific markers (warfarin, phenylbutazone, azapropazone) of albumin's drug-binding site I. However, instead of albumin's one high-affinity site/molecule, a mean value of 0.5 site/molecule was obtained with rat alpha 1-FP. Charcoal treatment at neutral pH of rat serum albumin did not affect its measured binding properties, but treatment of the alpha 1-FP led to an increased affinity for warfarin, phenylbutazone and azapropazone without a change in the measured number of sites, indicating competition for binding at this site by (an) endogenous ligand(s). These results are discussed in terms of the structures of the two proteins and with respect to the physiological implications of the differences found.
Animals↗
Identification of copper- and zinc-binding ligands in human and bovine milk.
The object of this study was to identify copper and zinc ligands detected during modified gel chromatography ( MGC ) of bovine and human milk ultrafiltrates. Isolation by anion-exchange chromatography and subsequent proton nuclear magnetic resonance (NMR) spectroscopy analysis demonstrated that the sole major low-molecular-weight ligand binding copper and zinc in bovine milk is citrate. Human milk apparently also contains citrate as a major metal-binding ligand but also contains amino acids, of which primarily glutamate was purified by anion-exchange chromatography. The amino acids bind copper well but are weak zinc-binding ligands. An artifactual MGC peak was seen in the milks, which was shown to be caused by the calcium present in the milk samples. No major differences in zinc-binding capacity were demonstrated between the low-molecular-weight fractions of the two milks. Although citrate may play a role in zinc uptake, it is apparently not the difference between the milks crucial to the acrodermatitis enteropathica individual. The difference in zinc availability between the milks may lie in some other aspect such as binding by proteins, which were noted to bind metal during MGC of nonultrafiltered milks.
Amino Acids↗
Magnification factors from an intracardiac marker.
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Cardiac Catheterization↗
Metal-binding ligands in Viokase.
The object of this study was to detect low molecular weight zinc binders in Viokase, a porcine pancreatic preparation used in the treatment of variant acrodermatitis enteropathica (AE). Extracts were centrifuged and ultrafiltered to yield a soluble fraction containing solutes of molecular weights less than or equal to 500 daltons. These were studied by modified gel chromatography (MGC) using sealed Sephadex G-15-120 columns equilibrated with buffered solvent systems containing either 5 ppm copper (II) or 5 ppm zinc (II). Eluted fractions were assayed for these metals by atomic absorption and for amino acids by various techniques. MGC profiles of ultrafiltrates resulted in a peak consisting of glutamic acid and another peak consisting of several amino acids. A third peak was due to metal ions. Citrate and picolinate have been claimed to be important zinc-binding ligands in Viokase, but neither was detectable by MGC, although small amounts of citrate or similar compounds were detected by the Furth and Herrmann reaction. Since amino acid ligands are easily detectable by MGC, and metal distribution among ligands is competitive in nature, the possibility of a role for citrate or picolinate as a zinc transporter in Viokase is seriously reduced. Relief to the variant AE patient was probably not due to citrate- or picolinate-enhanced zinc uptake.
Acrodermatitis↗
Pharmacokinetics of chloramphenicol in the neonatal horse.
Chloramphenicol sodium succinate was administered as an intravenous bolus (50 mg/kg) to eight foals which weighed 49-57 kg (mean +/- 1 standard deviation = 53.19 +/- 2.66) each, and were 1-9 days (4.5 +/- 2.56) of age. The drug was rapidly distributed and followed first-order elimination. Mean pharmacokinetic values were: zero-time serum concentration (C0) = 36.14 microgram/ml (+/- 14.80); apparent specific volume of distribution (Vd) = 1.614 1/kg (+/- 0.669); and elimination rate constant (K) = 0.7295 h-1 (+/- 0.3066) which corresponds to a biological half-life (t1/2) = 0.95 h. These values do not differ greatly from those reported for adult horses and ponies. A suspension of chloramphenicol was administered by nasogastric tube (50 mg/kg) to a second group of seven foals which weighed 49 to 57 kg (51.34 +/- 2.82) each and were 1 to 7 days (4.43 +/- 1.90) of age. A mean peak serum chloramphenicol concentration of 23.97 microgram/ml (+/- 7.06) was achieved 1.14 h (+/- 0.63) after administration. The bioavailability of this preparation was 83.27 percent.
Animals↗
An improved formulation of Nocht's azure-eosin stain for plastic embedded material.
The popular azure-eosin stain of Nocht has been reformulated to provide consistent, intense staining of semithin sections of water-miscible methacrylate embedded tissues.
Animals↗
Pre-embedding immunohistochemistry as an approach to high resolution antigen localization at the light microscopic level.
Pre-embedding immunohistochemistry with subsequent embedding in hydroxypropyl methacrylate enables one to obtain high resolution staining of antigens in 1 mu tissue sections. A routine method using formaldehyde fixation, methanol permeation, and an indirect method with fluorescein-labeled second antibody is described. This method is compared with other pre-embedding staining procedures. To illustrate the method the mouse small intestine was chosen as a model and stained with antibodies to tubulin, actin, and fibronectin. Some anticipated and some unusual staining patterns were found.
Actins↗
Detection of low molecular weight copper(II) and zinc(II) binding ligands in ultrafiltered milks-the citrate connection.
Low molecular weight zinc(II) and copper(II) binding ligands were detected in ultrafiltered human, bovine, and goat milk by the application of the method of modified gel chromatography. Human milk contains at least three detectable low molecular weight copper binders, whereas bovine and goat milk contain at least two. All three milks show two copper binding peaks with the same elution volumes. Zinc chromatograms were less specific than copper. Zinc showed only a single detectable low molecular weight binding ligand common to all three milks. Elution volumes of both zinc (II) and copper(II) citrate and picolinate systems were measured. Elution volumes of both copper II and zinc(II) citrate complexes are identical to elution volumes of an intense peak observed with all three milks; it is reasonable to assume that at least part of this peak corresponds to citrate. Human milk alone has a relatively intense binding peak for copper(II) at the same elution volume as the glutamate complex. Human and goat milk have another low intensity copper(II) binding ligand peak at the same elution volume; a number of amino acid complexes have binding peaks at this position. No peak characteristic of the zinc(II) or copper(II) picolinate systems could be found with any of the milks.
Animals↗
A simple procedure for extracting methacrylic acid from water-miscible methacrylates.
A simple procedure for removing methacrylic acid from water-miscible methacrylates is described. One volume of monomer is diluted with 9 volumes of diethyl ether. Three consecutive extractions are carried out with 5% aqueous NaHCO3 at 4 C. Residual water is removed by shaking with anhydrous sodium sulfate. The ether is removed by flash evaporation on a Büchi Rotavapor. Weak alkali extraction produces good quality semithin sections which are free of background staining. This method may be a useful alternative to existing methods for removal of methacrylic acid.
Acrylates↗