Reference

Spectroscopic studies of explosives

Spectroscopic studies of explosives. 1. Detection of nitro compounds on silica gel and carbon by nonresonant Raman spectroscopy. Carver, F. W. S.; Sinclair, T. J. (Minist. Defence, RARDE, Sevenoaks TN14 7BP, UK). J. Raman Spectrosc., 14(6), 410-14 (English) 1983. CODEN: JRSPAF. ISSN: 0377-0486.There are some commonly used reagents with their cas registry numbers 121-82-4 and 55-63-0 in this article. DOCUMENT TYPE: Journal CA Section: 50 (Propellants and Explosives) Raman spectra were obtained from trace amts. of nitroglycerin [55-63-0], PETN [78-11-5], RDX [121-82-4], and TNT [118-96-7] adsorbed on silica gel and on activated charcoal. The detection limits for these nitro compds. were 1-10 mg on silica gel and 20-40 ng on activated charcoal. .

Characterization of the thrombin-induced contraction of vascular smooth muscle

Characterization of the thrombin-induced contraction of vascular smooth muscle. Haver, Virginia M.; Namm, Donald H. (Dep. Pharmacol., Burroughs Wellcome Co., Research Triangle Park, NC, USA). 15078-28-1 and 55-63-0 are cas registry numbers. These chemicals are also mentioned in this article. Blood Vessels, 21(2), 53-63 (English) 1984. CODEN: BLVSAB. ISSN: 0303-6847. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Section cross-reference(s): 1 Purified human a-thrombin induced a sustained contraction of isolated rabbit aorta and dog coronary arteries. These vascular tissues also exhibited a refractoriness towards a 2nd thrombin exposure. The extent of tachyphylaxis exhibited by the aorta correlated with the initial concn. of thrombin and the length of time the tissue was exposed to thrombin. The thrombin-induced contraction in the aorta was not blocked by phospholipase or cyclooxygenase inhibitors, but it was inhibited in the presence of hirudin, heparin, nitroglycerin, and nitroprusside. Nitroglycerin, nitroprusside, and hirudin also inhibited the contraction in the dog coronary artery. Ca2+-channel blockers did not inhibit the thrombin-induced contraction in the coronary artery, although a small inhibition was obsd. in Ca2+-free media. In both tissues, equiv. contractile responses were obtained using equimolar quantities of b-, tetranitromethane-, and a-thrombin, even though the latter's coagulant activity was 30-40-fold that of the modified thrombins. However, if the catalytic activity of thrombin was inhibited by modification with TLCK, hirudin, or heparin/antithrombin III, the vasoconstrictor activity was also lost. Evidently, alterations of the fibrinogen-binding site do not affect the contractile activity of thrombin. The contraction may be the result of a proteolytic interaction of the active site of the enzyme with vascular smooth muscle. .