Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0086543 (cataract)
 29,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lipid extracts of the human cataractous and normal lenses were analyzed by thin-layer chromatography (TLC) using a solvent system consisting of CHCl3/CH3OH/CH3COOH/H2O (50:25:7:3 by vol.). A novel phospholipid having a Rf intermediate between phosphatidyl ethanolamine (PE) and phosphatidyl serine (PS) was detected besides the four major phospholipids viz., PE, PS, phosphatidyl choline (PC) and sphingomyelin (SP). The novel phospholipid was found to be molybdenum positive and ninhydrin negative having a characteristic fluorescence of Schiff-base conjugate formed between PE, malondialdehyde (MDA) and PS. It was possible to resolve this adduct into PE and PS after acid hydrolysis using two dimensional TLC with CHCl3/CH3OH/NH3 (7 M) (65:25:4 by vol.) as the second solvent. In cataract PE . MDA . PS adduct increased significantly as did diene conjugates and MDA. In plasma membrane lipid extract of cataractous lenses there was a marked increase in fluorescence at 460 nm when excited at 365 nm showing a characteristic fluorescence of a typical Schiff-base conjugate. The evidence suggests that peroxidation of lenticular plasma membrane lipids is one of the molecular mechanisms involved in cataract in the human.
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PMID:Molecular mechanisms of cataractogenesis: IV. Evidence of phospholipid . malondialdehyde adduct in human senile cataract. 372 54

In this article, the surface of intraocular len material PMMA was first aminated for activation on which some polar groups generated such as C-N, COO(-), -OH, NH3(+), etc. Then the anticoagulant drugs recombinant hirudin (rH) was grafted with amido bonds to look forward to resist the adsorption of nonspecific protein or cells in tear, even the cataract. The detailed analysis and discussion about the grafting quantity, molography, wettability, electric charges, chemical structure, and the dynamic adsorption of protein Fn on the material surface were carried on by the technology of ultraviolet photometric, contact angle, solid Zeta potential, X-ray photoelectron spectroscopy, and quartz crystal microbalance. The surface with a certain amount of rH modification existed more hydrophilic due to the amphiphilic structure than before, on which the protein adsorption was the most unstable. The results indicated that the rH modification improved the resistance of PMMA to nonspecific adsorption of protein Fn to achieve the expectative effect.
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PMID:Biological protein-resistance layer construction of recombinant hirudin on polymethyl methacrylate IOL surface. 2482 86