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Страница 1 од 311 резултати
Lens proteases.
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Lens proteases and cataract formation.
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Naphthol and lens.
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Alpha and beta naphthols, the metabolites of naphthalene, a cataractogenic agent, was tested for it's effect on sheep lens proteases and their inhibitors. It reduced protease activities, not that of inhibitor activities of lens proteins. It also increased the efflux of free amino acid from lenses
Lens hydration in transgenic mice containing HIV-1 protease linked to the lens alpha A-crystallin promoter.
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Two constructs of transgenic mice, TG61 and TG72, containing HIV-1 protease linked to lens alpha A-crystallin promoter develop cataract. The TG61 construct exhibits cataractogenesis in utero, while in the TG72 construct frank opacities appear 24 days (homozygotes) and 26 days (hemizygotes) after
The occurrence of proteases in bovine lens.
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Bovine lens calmodulin. Isolation, partial characterization and calcium-independent binding to lens membrane proteins.
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Calmodulin has been isolated from calf lens fiber cells. Like other vertebrate calmodulins lens calmodulin shows a calcium-dependent mobility shift on SDS-polyacrylamide gels and forms immune complexes with antiserum, raised against vertebrate calmodulin. Via the gel overlay technique radioiodinated
Phosphorylation of lens membranes with a cyclic AMP-dependent protein kinase purified from the bovine lens.
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We report the phosphorylation of lens membranes with a cAMP-dependent protein kinase isolated from bovine lenses. The holoenzyme was eluted from DEAE agarose at less than 100 mM NaCl and from gel filtration columns with a relative molecular weight of 180 000. The regulatory subunit was identified
N-cadherin of the human lens.
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N-cadherin was identified in the human lens by its immunological specificity, and concanavalin-A (Con-A) binding. The 135 kd glycoprotein was partially purified from human lens plasma membranes by Con-A affinity column chromatography. In the newborn lens, N-cadherin is distributed equally in amount
Regulation of lens connexin 45.6 by apoptotic protease, caspase-3.
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Gap junctions are important in maintaining lens homeostasis. Here we report that connexin 45.6 (Cx45.6) was partially truncated to a 46 kDa fragment during chicken lens development. This specific truncation initiated during embryonic days and the truncated fragment accumulated towards the later
Characterization of a bradykinin-hydrolyzing protease from the bovine lens.
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OBJECTIVE
To isolate and characterize bovine lens endopeptidase activity that cleaves the Phe-Ser bond in peptide substrates.
METHODS
The protease activity in young bovine lens homogenate was measured using the Mca-(Ala(7),Lys(Dnp)(9))-bradykinin substrate. Degradation of bradykinin and other
Human senile cataractous lens protease. Isolation and some chemical characteristics.
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A proteolytic enzyme was isolated from human senile cataractous lens by anion-exchange and gel-filtration chromatography. Sedimentation and zone-electrophoretic experiments indicated a high degree of homogeneity for the enzyme. A molecular weight of 27000 was calculated from measurements of
Comparison of virulence factors in Pseudomonas aeruginosa strains isolated from contact lens- and non-contact lens-related keratitis.
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Pseudomonas aeruginosa is one of the common pathogens associated with corneal infection, particularly in contact lens-related keratitis events. The pathogenesis of P. aeruginosa in keratitis is attributed to the production of virulence factors under certain environmental conditions. The aim of this
Evidence for a calcium activated protease specific for lens intermediate filaments.
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The calcium mediated loss of intermediate filament protein from lens cytoskeletal preparations was examined by soft laser scanning densitometry of polyacrylamide gels. The time course of proteolysis by the lens Ca++ activated proteinase and inhibition by EGTA or PMSF and leupeptin were also
Calpain in cultured bovine lens epithelial cells.
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Calcium dependent proteolysis was examined in supernatant prepared from cultured bovine lens epithelial (BLE) cells. The presence of the calcium activated protease, calpain, was indicated by immunorecognition of 80 kDa and 30 kDa subunits of calpain in BLE cell supernatant. Degradation of
Biochemical properties of lens-specific calpain Lp85.
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Lens-specific Lp82 and ubiquitous m-calpain are neutral, calcium-activated, cysteine proteases. Both calpains are activated during rodent lens maturation and cataract formation. Lp85 calpain (Lens protein with MW=85 kDa) is a slightly larger splice variant of Lp82. Lp85 contains a 28 amino acid
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