Reference

Low dose measurements with lyoluminescence materials

Low dose measurements with lyoluminescence materials. Busuoli, G.; Monteventi, F.In this study， 3458-28-4 and 50-99-7 are also used. (ENEA, Bologna 40138, Italy). Radiat. Prot. Dosim., 6(1-4), 172-4 (English) 1984. CODEN: RPDODE. ISSN: 0144-8420. DOCUMENT TYPE: Journal CA Section: 71 (Nuclear Technology) Section cross-reference(s): 73 Lyoluminescence (LL) measurements are reported for which the reader assembly was improved to standardize the measurement procedures and to limit the uncertainties. Materials, such as L-glutamine [56-85-9] and N-acetyl-D-glucosamine [7512-17-6], in addn. to mannose [3458-28-4] and glucose [50-99-7], were tested by using sensitized solns. heated and kept at const. temp. during the read-out process. Mannose is rather insensitive, even when using sensitized solns. (min. detectable dose: 0.1 Gy), while the detection limit for glucose and N-acetyl-D-glucosamine is of the order of 2 mGy using luminol [521-31-3] as the sensitizer. The reproducibility is within ±10% for doses of the order of 50 mGy for glucose. Measurements with diphenylisobenzofuran [5471-63-6] showned small amplification of the LL signal. .

Characterization of muscarinic acetylcholine receptors as glycoproteins

Characterization of muscarinic acetylcholine receptors as glycoproteins. Yagisawa, Hitoshi; Yamagishi, Shunichi; Sugiyama, Hiroyuki (Lab. Membr. Biol., Natl. Inst. Physiol. Sci., Okazaki 444, Japan). Proc. Jpn. Acad., Ser. B, 59(9), 324-7 (English) 1983. CODEN: PJABDW. ISSN: 0386-2208. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Muscarinic acetylcholine [51-84-3] receptors (mAChRs) solubilized from porcine brain mitochondria bound to wheat germ agglutinin (WGA) and slightly to con A [11028-71-0] but not at all to several other lectins coupled to Sepharose 4B. Binding to WGA was completely inhibited by N-acetylglucosamine [7512-17-6]. Further chromatog. anal. revealed the presence of 2 populations of mAChRs, a major one which binds to WGA and a minor one which cannot bind the lectin. Apparently, a structural heterogeneity of the receptors exists regarding their glycosyl residues.