Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.4 (chondroitinase)
 2,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study continues previous research to confirm that glycosaminoglycans (GAGs) exert a positive effect on promoting iron uptake by Caco-2 cells. Cooked haddock was digested with papain, and GAGs were further purified on the basis of their sulfur content. Reverse phase chromatography (RP-HPLC) and digestion with chondroitinase ABC (Chase) (50 mU/mg) were used to approach the identification of the GAGs. FeCl 3 was mixed with the purified GAGs, and Fe uptake was measured by ferritin formation using an in vitro digestion/Caco-2 cell model. The identificative analyses suggest that chondroitin/dermatan sulfate-related structures promote Fe uptake by Caco-2 cells; however, this effect was lower (40%) than that observed with whole fish muscle. Chase eliminated the positive effect on Fe uptake. These results indicate that specific GAGs may contribute to the enhancing effect of meat on Fe absorption. Further in vivo studies addressing these aspects of the meat factor are needed.
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PMID:Isolated glycosaminoglycans from cooked haddock enhance nonheme iron uptake by Caco-2 cells. 1885 Jul 15

Glycosaminoglycans (GAGs) including chondroitin sulfate (CS) and chondroitin sulfate/dermatan sulfate (CS/DS) copolymers are anionic straight chain polysaccharides. They are galactosamine containing GAGs (galactosaminoglycans) having wide range of applications in pharmaceutical, cosmetic and food industries. This article reviews techniques to isolate and characterize these galactosaminoglycans from animal and poultry tissues. Patent based information is also discussed. Cartilaginous tissues are the major source of CS consisting entirely of D-glucuronosyl-N-acetylgalactosamine repeating disaccharide units, in which the galactosamine is sulfated at C4 or C6. In contrast, most galactosaminoglycans in non-cartilaginous connective tissues (e.g. skin and tendon) are CS/DS copolymers comprised of varying proportions of D-glucuronosyl-N-acetylgalactosamine and L-iduronosyl-N-acetylgalactosamine. Tissues are digested with proteinase (e.g. papain) to liberate GAGs, which are fractionated to isolate and purify galactosaminoglycans. Common techniques used for fractionation of GAGs include: precipitation with different concentrations of ethanol; solubilization of GAG precipitated as GAG-quarternary ammonium compound complexes with different concentrations of NaCl; anion exchange chromatography and gel filtration chromatography. Purified galactosaminoglycans are examined by various methods including chondroitinase digestion, high performance liquid chromatography and electrophoresis. Histological methods are used to localize galactosaminoglycans in tissues. The patent information on the CS hydrolase and ultraviolet irradiation may be useful for the preparation of CS oligosaccharide.
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PMID:Extraction, isolation and analysis of chondroitin sulfate glycosaminoglycans. 2065 51

In order to advance the development of cryopreservation and other assisted reproductive technologies in camelids it is necessary to eliminate the viscous component of the seminal plasma without impairing sperm function. It has been postulated that glycosaminoglycans (GAGs) or proteoglycans are responsible for this viscosity. This study investigated the effect of the GAG enzymes hyaluronidase, chondroitinase ABC and keratanase and the proteases papain and proteinase K on seminal plasma viscosity and sperm function in order to aid identification of the cause of seminal plasma viscosity and propose methods for the reduction of viscosity. Sperm motility, DNA integrity, acrosome integrity and viability were assessed during 2h incubation. All enzymes reduced seminal plasma viscosity compared to control (P<0.001) although papain was most effective, completely eliminating viscosity within 30 min of treatment. Sperm motility and DNA integrity was not affected by enzyme treatment. The proportion of viable, acrosome intact sperm was reduced in all enzyme treated samples except those treated with papain (P<0.001). These findings suggest that proteins, not GAGs are the main cause of alpaca seminal plasma viscosity. Papain treatment of alpaca semen may be a suitable technique for reduction of seminal plasma viscosity prior to sperm cryopreservation.
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PMID:The effect of glycosaminoglycan enzymes and proteases on the viscosity of alpaca seminal plasma and sperm function. 2353 79


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