Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Activity of tissue and blood plasma kallikreins as well as total content of their inactive precursors were studied in rabbit eye structures and media: iris, ciliary body, cornea, vascular striatum, retina, aqueous humor, tear liquid, lacrimal gland by means of fluorimetric procedure using Z-Phe-Arg-MCA as a substrate. Dissimilar capacity of the trypsin soya bean inhibitor and of aprotinin (basic inhibitor of Kunitz type) to inhibit tissue and blood plasma kallikreins enabled to differentiate the enzymatic activity. Lacrimal gland contained the highest activity of tissue kallikrein which amounted to 70% of total Z-Phe-Arg-MCA-hydrolyzing activity of the homogenate. Total Z-Phe-Arg-MCA-amidase activity and activity of individual kallikreins was distinctly lower in all the eye structures and media studied as compared with that of lacrimal gland. Activity of tissue kallikrein was higher than blood serum kallikrein activity in iris, ciliary body, vascular striatum, retina and conjunctiva. The highest content of prekallikreins was found in conjunctiva, aqueous humor, iris and ciliary body. Tissue and blood plasma kallikrein-kinin systems appear to carry out dissimilar functions in eye tissue structures; they are apparently involved in pathogenesis of some eye diseases.
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PMID:[Activity of tissue and plasma kallikrein and level of their precursors in eye tissue structures and media of healthy rabbits]. 172 76

Using human and bovine corneal tissue, we investigated the in vitro metabolism of bimatoprost (17-phenyl-18,19,20-trinor-prostaglandin F(2alpha) ethyl amide, Lumigan (Allergan, Inc, Irvine, CA). Enzymatic amidase activity, which converts bimatoprost to the corresponding prostaglandin carboxylic acid, was found to be present in corneal tissue from both species. Using HPLC and mass spectrometry for analyses, conversion of bimatoprost to 17-phenyl-18,19,20-trinor prostaglandin F(2alpha) continued for at least 24 hours after excision of the cornea, with a conversion rate of approximately 25 microg/24 hours. This hydrolysis product is identical to the free acid of latanoprost with the exception of a double, rather than a single, bond at the carbon 13-14 position. Assuming that this conversion also occurs in vivo at a similar rate, this hydrolysis product may account for the reduction of intraocular pressure occurring in patients treated with bimatoprost.
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PMID:The hydrolysis of bimatoprost in corneal tissue generates a potent prostanoid FP receptor agonist. 1220 99