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Biomedical subjects

R H Glew

Publications and source records attributed to R H Glew.

At least 253 records · Page 14Linked to original sources
PubMed1973

Enzyme loading of erythrocytes.

We demonstrated that beta-glucosidase and beta-galactosidase can be trapped inside erythrocytes by rapid hemolysis of the cell in the presence of these enzymes. Enzyme enters only during hemolysis, and optimum uptake occurs within 60 sec. There is no loss in cell number after hemolysis-induced enzyme uptake, and the ghosts have only a slightly increased mean cell volume. Smaller proteins enter more readily than larger proteins, although enzymes with a molecular weight of at least 180,000 can be readily entrapped by erythrocytes. This finding may provide a useful approach to the problem of enzyme replacement in certain diseases, including Gaucher's disease.

Animals↗
PubMedDate not supplied

Naegleria lovaniensis tarasca new subspecies, and the purepecha strain, a morphological variant of N. l. lovaniensis, isolated from natural thermal waters in Mexico.

Amoebae were isolated from a natural thermal water source in Michoacán, Mexico, in September 1986. Two 500-ml samples were taken from pools with water at 45 degrees C and 46 degrees C and concentrated at 2,000 g for 15 min. The sediment was seeded on nonnutritive agar plates and incubated at 42 degrees C. The isolates were axenized in bactocasitone-serum medium. The identification of the isolates was based on their morphology, total protein and isoenzyme patterns by agarose isoelectric focusing, serology, fine structure, agglutination with Concanavalin A, sensitivity to trimethoprim, capacity to kill mice, and their cytopathic effect in Vero cells. The results showed several morphophysiological, biochemical and serological differences between the isolates and the type strain Aq/9/1/45D of Naegleria lovaniensis. These remarkable differences provide sufficient evidence to consider one of the isolates a new subspecies, and the other one a morphological variant of N. l. lovaniensis, which can be differentiated from other Naegleriae by their morphology, biochemistry, serology and physiology. The authors propose the name tarasca for the subspecies and purepecha for the morphological variant.

Amebiasis↗
PubMedDate not supplied

Lysosomal hydrolases in middle ear effusions.

Biochemical studies of middle ear effusions have demonstrated generally higher levels of certain hydrolytic and oxidative enzymes in mucoid fluids when compared to serous. We have extended these studies by analyzing middle ear effusions for the content of a large number of lysosomal hydrolases. The mean specific activity for alpha-glucosidase in mucoid fluids was found to be ten times that for serous fluids while alpha-mannosidase, beta-glucuronidase, hexosaminidase, acid phosphatase, beta-galactosidase, alkaline phosphatase, and lactate dehydrogenase were found to be three to five times greater in mucoid than serous effusions. In this study the specific enzyme activities for lysosomal hydrolases from purulent effusions were found to be intermediate between the activities in serous and mucoid effusions. No significant correlation was found between the specific activities of lysosomal hydrolases and the presence or absence of bacteria in mucoid or serous middle ear effusions. The hexosaminidase isozyme distribution was found to be identical for serous and mucoid fluids and similar to that found in human serum. However, the isozyme pattern of beta-glucuronidase in mucoid effusions was significantly different than that in normal human serum as mucoid fluids contain a large amount of an anionic isoenzyme of beta-glucuronidase that is barely detectable in human serum.

Adolescent↗
PubMedDate not supplied

Neuraminidase activity in middle ear effusions.

Analyses of Streptococcus pneumoniae culture filtrates and middle ear effusions (MEE) containing S pneumoniae for various hydrolytic enzymes have demonstrated substantial levels of neuraminidase activity when measured employing a sensitive fluorometric assay. S pneumoniae neuraminidase exhibits optimum activity near neutral pH (6.0 to 6.5), and catalyzes the cleavage of sialic acid residues from glycoproteins, gangliosides and mucopolysaccharides. S pneumoniae begins secreting large amounts of neutral neuraminidase (mean [means] = 43.3 units/mL culture filtrate) when cells enter the stationary phase. Nearly all (96%) human chronic MEEs yielding positive cultures for S pneumoniae contain neuraminidase activity (means = 0.200 units/mg protein), while only 21.1% to 45.5% of all other effusions contain the enzyme. Middle ear effusions obtained from S pneumoniae infected-chinchillas contained large amounts of neuraminidase activity (approximately 200 units/mL), which decayed exponentially in vivo with an apparent half-life of 8 1/2 days. Three neuraminidase isoenzymes (designated I-III) were identified in S pneumoniae culture filtrates, as well as in MEEs from chinchillas infected with the organism, using a combination of ion-exchange and gel filtration chromatography. With 4-methylumbelliferyl-N-acetylneuraminic acid serving as substrate, preparation I from both culture filtrates and MEEs was characterized by a high Michaelis constant (Km), while forms II and III had low Km values. Preferred substrates were orosomucoid and neuramin-lactose; gangliosides, thyroglobulin, and bovine submaxillary mucin were poorer substrates.

Animals↗
PubMedDate not supplied

Experimental alteration of chinchilla middle ear mucosae by bacterial neuraminidase.

Streptococcus pneumoniae secretes a variety of extracellular glycosidase including a neuraminidase which has been found in middle ear effusion from patients with both acute and chronic otitis media. This enzyme cleaves sialic acid from membrane glycoproteins, thereby exposing galactose residues, the penultimate sugar. The ability of partially purified neuraminidase to alter the middle ear mucosa was investigated in the chinchilla. After incubation with neuraminidase, chinchilla middle ears were removed and exposed to galactose residues labeled with tritium. Membrane glycoproteins were solubilized and separated according to molecular weight by sodium dodecylsulfate electrophoresis. Increases in tritium incorporation, when compared to control incubations, indicated that galactose residues had been exposed and sialic acid residues removed from glycoproteins of both high and low molecular weight. Such membrane destruction could contribute significantly to the pathology of otitis media with effusion.

Animals↗
PubMedDate not supplied

Parenteral feeding alters the fatty acid composition of serum phospholipids of rabbits.

BACKGROUND: Cholestatic liver disease develops in 30% to 70% of neonates receiving total parental nutrition (TPN). We analyzed the fatty acid composition of serum phospholipids from control and TPN-fed rabbits to determine if TPN altered the fatty acid profile. METHODS: Eleven male New Zealand White rabbits aged 9 to 11 weeks received TPN, whereas 11 other rabbits were offered standard laboratory rabbit chow ad libitum. After 14 days on the prescribed diet, serum samples were analyzed for their phospholipid fatty acid content by gas chromatography. RESULTS: The proportions of palmitolenic (16:2n7), alpha-linolenic (18:3n3), arachidic (20:0), and eicosaenoic (20:1n9) acids were significantly lower in the serum phospholipids of the TPN-fed animals compared with the control group. The proportion of docosahexaenoic acid (22:6n3), a fatty acid that is critical to the development of the nervous system, was increased two- to threefold. CONCLUSIONS: The differences in proportions of fatty acids observed between control and TPN-fed animals indicate that a fatty acid elongation and desaturation pathways are perturbed in rabbits on TPN.

Amino Acids↗