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Reference
- Activated, stabilized enzymes useful for wound healing
- Activated, stabilized enzymes useful for wound healing. Bilton, Gerald L. (Hafsten, Raymond, J., Jr., USA). PCT Int. Appl. WO 8402274 A1 21 Jun 1984, 21 pp. DESIGNATED STATES: W: JP; RW: AT, BE, CH, DE, FR, GB, LU, NL, SE. (English). (World Intellectual Property Organization). CODEN: PIXXD2. CLASS: IC: A61K037-62. APPLICATION: WO 83-US1922 7 Dec 1983. PRIORITY: US 82-448154 9 Dec 1982. DOCUMENT TYPE: Patent CA Section: 63 (Pharmaceuticals) A stable enzyme compn. contains proteolytic enzymes in an amt. effective to produce a fibrinolytic effect at a wound site, an amt. of starch [9005-25-8] effective to immobilize the enzymes, amino acids, and a raw gland or organ conc. Part A of a compn. was prepd. contg. thymus substance 1.5, spleen substance 1.5 L-arginine HCl [15595-35-4] 0.5, L-lysine-HCl [10098-89-2] 0.5, DL-methionine [59-51-8] 0.5, L-glutamic acid [56-86-0] 0.5, L-leucine [61-90-5] 0.5, glutatione [70-18-8] 0.5, and L-arginine-L-glutamate [4320-30-3] 0.5 kg. Part B contained pancreatin [8049-47-6] 5.7, papain [9001-73-4] 7.3, bromolain [9001-00-7] 5.8, ficin [9001-33-6] 2.0, trypsin [9002-07-7] 0.3 and chymotrypsin [9004-07-3] 0.7 kg. Part C contained Mg stearate 1.5, alginic acid 1.5, Ca bicarbonate 1.5, starch 3.0 and CaHPO4 33.8 kg. Part A was mixed at low humidity and ingredients of Part B sequentially added while lightly spraying 7.4 g of 24.0 mL refined food glaze in 16.7 mL iso-PrOH. Part C ingredients were then added and the powd. compn. compressed into tablets and enteric coated.
- Protective effect of arginine in hyperoxia
- Protective effect of arginine in hyperoxia. Activity of glutaminase and glutamate decarboxylase in the brain. Krichevskaya, A. A.; Shugalei, V. S.; Tsvetnenko, E. Z.; Ananyan, A. A. (Rostov State Univ., Rostov-on-Don, USSR). Vopr. Med. Khim., 24(1), 42-6 (Russian) 1978. CODEN: VMDKAM. ISSN: 0042-8809. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Interactions) Hyperoxia (6 atm.) decreased the activities of phosphate-dependent and phosphate-independent glutaminase [9001-47-2] and glutamate decarboxylase [9024-58-2] in the rat cerebral cortex by 45, 51, and 32%, resp. When injected 30 min before induction of hyperoxia, L-arginine-HCl [15595-35-4] (100 mg/100 g, i.p.) delayed the development of O spasms and increased the brain glutamate dehydrogenase activity to 29% above the normal level. Glutaminase activity was unaffected by arginine.
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