PubMed · 2885789
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
S Conigliaro, R Rosà, F Osimo, E Fumagalli, G Cavaliere, G Arrigo. 1987-07-31. [Chronic headache].. https://pubmed.ncbi.nlm.nih.gov/2885789/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Significant differences in urinary excretion of N-acetyl-beta-glycosaminidase (NAG) were observed between nulliparous and multiparous patients and between fasted and nonfasted individuals. No significant difference was observed between patients with normal and those with abnormal glucose tolerance. Multiple regression analysis confirmed that the significant independent determinants of NAG/creatinine ratio were age, parity, gestation and fasting state. Significant diurnal variation in urinary NAG/Cr ratio was observed, the highest levels being recorded in early morning fasting specimens, falling in each postprandial specimen and beginning to rise again by midnight. The urinary NAG/Cr ratio is influenced by fasting, parity, gestation and age. More consistent results for prediction of pre-eclampsia are therefore likely to be obtained using fasting (early morning) urine specimens and adjusting cut-off criteria for the other factors.
We imaged the horizontal semicircular canal (HSCC) crista and cupula of toadfish, Opsanus tau, by using a) confocal light microscopy of isolated vital HSCC; b) serial sections of fixed, trichrome-stained HSCC; and c) scanning electron microscopy of fixed HSCCs. HSCC were dissections which included an ampulla and an attached canal tube (long and slender canal portion), and, in some cases, a small portion of the utricular wall. Cupulae were seen as multipartite mucus connective tissue shells rising from the crista and extending toward the ampullary roof. They were composed of several refractile bands traversing the cupulae perpendicular to longitudinal fibers extending from the cupular base to its apex. Alcian green-stained cupulae showed an asymmetric alcianphilic, dark, X-shaped structure, indicating that the pillar is rich in mucin and carbohydrate, an interpretation supported by images of trichrome-stained sections. The cupular antrum is devoid of prominent refractile fibers. No tubes or channels were observed in the cupula or antrum of vital preparations. Cupular shell fibers cover the surface of the crista, are roughly parallel, and are associated with a translucent material having a refractive index greater than the surrounding endolymph. Stereocilia were thin, 100-microm-long structures, with little longitudinal curvature, which end with no end bulb. No strands extend from stereocilia to the roof or other portions of the cupular antrum. Gross movements of stereocilia were not seen in mechanically quiescent preparations. Within the cupular antrum, stereocilia were parallel to connective tissue fibers, all embedded in an isotropic gel. This fiber-reinforced gel and cupular matrix are sensitive to N-acetlyneuraminidase and beta-N-acetyl glucosaminidase, and minimally sensitive to beta-N-acetyl hexosaminidase. Connective tissue fibers may serve to stiffen the gel, whose matrix would restrict lateral motion of embedded fibers and stereocilia thereby providing mechanical support for stereocilia.
An exo-N-acetyl-beta-d-glucosaminidase from the thermotolerant Bacillus sp. NCIM 5120 was purified to homogeneity by chromatography on CM-cellulose, Sephacryl S-300 and phenyl-Sepharose. The enzyme has a Mr of 230000 as determined by size exclusion chromatography on Sephacryl S-300/Sephadex G-200 and exhibited a relative subunit Mr of 60000 on denaturing gel electrophoresis. It is a neutral protein with a pI of 6.79. The optimum pH and temperature for the enzyme activity are 6.0 and 70 degreesC, respectively. Determination of the reaction stereochemistry indicates that the enzyme is a retaining glycosidase with the beta anomer of GlcNAc formed as the initial product. Determination of the energy of activation with different leaving groups (p-nitrophenol and 4-methyl-umbelliferone) reveals that the enzyme exhibits a biphasic Arrhenius plot with two characteristic energy of activation with an inflection temperature of 50 degreesC. The activation energy at temperatures below the inflection point was found to be higher than that above the inflection point. The energy of activation for 4-Me-Umb-beta-d-GlcNAc was higher at temperatures below the inflection point than for pNP-beta-d-GlcNAc (60.3 and 43.2 kJ mol-1, respectively). It hydrolyzes specifically, terminally linked beta(1-4) GlcNAc residues from the non-reducing end of oligosaccharides. Comparative studies on the hydrolysis of chito-oligosaccharides by the exo-N-acetyl-beta-d-glucosaminidase indicates that chitobiose is the best substrate with a Km and kcat of 0.34 mM and 24 microoff min-1mg-1, respectively. It also exhibits strict substrate specificity with respect to the glycone substitution as well as anomeric linkage.