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Lack of alpha-galactosidase activity in leukocytes has been linked to Fabry Disease. [2] Galactosidases have a variety of uses, including the production of prebiotics, the biosynthesis of transgalactosylated products, and the removal of lactose. B-galactosidase forms the basis of lac z operon in bacteria which can be used to control gene ...
Some species of bacteria, including E. coli, have additional β-galactosidase genes. A second gene, called evolved β-galactosidase (ebgA) gene was discovered when strains with the lacZ gene deleted (but still containing the gene for galactoside permease, lacY), were plated on medium containing lactose (or other 3-galactosides) as sole carbon ...
Colonies that produce β-galactosidase are turned blue by X-gal (5-bromo-4-chloro-3-indolyl-β-D-galactoside) which is an artificial substrate for B-galactosidase whose cleavage results in galactose and 4-Cl,3-Br indigo thus producing a deep blue color. [16] Allolactose is an isomer of lactose and is the inducer of the lac operon. Lactose is ...
Beta-galactoside permeases can describe any transport proteins that enable a cell to uptake, and thus accumulate, beta-galactosides. One known example of these transport proteins is the melibiose, or melB, carrier protein derived from the melB gene of E. coli. [3]
X-gal itself is colorless, so the presence of blue-colored product may therefore be used as a test for the presence of active β-galactosidase. This also allows for bacterial β-galactosidase (so called lacZ ) to be used as a reporter in various applications. [5] Similarly, Xαgal is used as a reporter compound for α-galactosidase (e.g. Mel1 ...
Senescence-associated beta-galactosidase, along with p16 Ink4A, is regarded to be a biomarker of cellular senescence. [1] [2] Its existence was proposed in 1995 by Dimri et al. [3] following the observation that when beta-galactosidase assays were carried out at pH 6.0, only cells in senescence state develop staining.
Anisha, G. S.; John, Rojan P.; Prema, P.; Pandey, Ashok (4 September 2008). "Investigation on α-Galactosidase Production by Streptomyces griseoloalbus in a Forcefully Aerated Packed-Bed Bioreactor Operating in Solid-State Fermentation Condition".
The lacZ fragment, whose synthesis can be induced by IPTG, is capable of intra-allelic complementation with a defective form of β-galactosidase enzyme encoded by host chromosome (mutation lacZDM15 in E. coli JM109, DH5α and XL1-Blue strains). [4] In the presence of IPTG in growth medium, bacteria synthesise both fragments of the enzyme.