Classic Galactosemia Type 1

Glyburide is another generic medication used in the management of diabetes mellitus type 2. Two trade names of this drug are DiaBeta and Glynase. The chemical name is 1-[ [p-[2-(5-chloro-o-anisamido) ethyl]phenyl]-sulfonyl]-3-cyclohexylurea. Doses up to 0.75-12 mg/day can be given as a single dose or divided doses. The circulation of the glyburide is that protein binding is extensive and half-life is 10 hours. It is excreted through the renal and biliary system. Glyburide acts as an oral blood glucose lowering drug. The drugs uses include binding and activating the sulfonylurea receptor 1, which causes depolarization. This results in an increase in intracellular calcium in the cells and stimulation of insulin release. Major drug interactions are noted between glyburide and

From these experiments, we were able to produce a standard curve, and a Lineweaver-Burk plot to determine Km (constant) and Vmax (maximal velocity). The turnover number (Kcat) was measured for pure beta- galactosidase from an assay at 280 nm absorbance. Additional we could determine the IPTG mechanism of inhibition, determine KI/KI’, and the optimal pH for beta- galactosidase.

First and foremost, the initial hypothesis of this experiment is that stevia, a plant-based and water-soluble sweetener, will inhibit the activity of the studied enzyme, α-amylase and that sucralose (i.e Splenda), an artificially produced sweetener, will have the opposite effect. Both stevia and sucralose designed for diabetics are expected to inhibit the activity of α-amylase more than sucrose. With this in mind, the results obtained from the experiment showed that stevia does indeed inhibit the activity of α-amylase most effectively compared to sucrose and sucralose. This can be explained by the small range of % inhibition values, ranging from 10-20 % inhibition. This can be observed in Figure 1 where one can notice that the standard error bars are

Gaucher’s disease is a lipid storage disease similar to Tay Sach’s because its deficiency of a lytic lysosomal enzyme. Gaucher’s disease is in regards to which parts of the body it affects. Tay Sach’s affects the CNS while Gaucher’s affects the spleen and liver. The main treatment option of Gaucher’s is enzyme replacement therapy (ERT). The deficient lytic enzyme (glucoserebrosidase) is injected intravenously and directed toward the lysosomes in

Hereditary fructose intolerance is an inborne error of fructose metabolism caused by missing an enzyme called adolase B.

The β-D-Galactose inhibitors were all made from β-D-Galactose pentaacetate (15), BF3 ∙ Et2O in DCM and three different alkyne containing alcohols (propargyl alcohol, 3-butyn-1-ol, and 4-pentyn-1-ol). Saturated aqueous NaHCO3 was used to neutralize the solution and after washing and drying the solvent was evaporated under reduced pressure to give the galactose inhibitors.

Regulation of DAG and phytoceramide by Ipc1. When Wild type and GAL7::IPC1 strains were exposed to galactose and glucose, DAG (activator of PKC1) levels in the GAL7::IPC1 strain increased when IPC1 was induced by galactose, and decreased when IPC1 was repressed by glucose. Furthermore, phytoceramide levels were increased when IPC1 was down regulated by glucose in the GAL7::IPC1 strain. In both wild type strains, no change was seen when IPC1 was up or down regulated, as expected (Fig. 2).

What is interesting about the disease is that it is the mutation in a single gene called GBA, in which prevents the production of an enzyme called Glucocerebroside (1). In our BIS 102 class, we have discussed the importance of enzymes since enzymes help speed up chemical reactions, especially in our body since enzymes are vital for our bodies to function. Without enzymes, some reactions may take years even hundreds years to react as with enzymes it may take a fraction of a second. Glucocerebrosidase is need to break down a type of lipid that is found in cell membranes called glucocerebroside (2). Glucocerebroside plays a big role in cell membrane since it links to many important functions such as cell to cell interaction, and regulation within the membrane. However, the liver and spleen tend to over produce glucocerebroside, and needs to be to be reduced into adequate amount to have a normal function, in which the enzyme glucocerebrosidase to degrade some of the lipid away. Gaucher disease prevents with the production of the enzyme, and the lipid will accumulate to a point in which affects the functions throughout

The results of this experiment suggest that an interaction is occurring between the EccA1 and the 4414 gene and that the regions responsible for the interaction are mainly N25 and N50. The N50 region of the 4414 gene might be where the interaction is occurring the strongest among the two regions. The CM –His –Trp –Ura plates with x-gal plate, Fig. 5, display the truncations on the left side as colored, indicating the production of b-galactosidase and that an interaction between the EccA1 and 4414 gene occurred. The columns in Fig. 5 that lack both EccA1 and 4414 gene and the top row that is missing only the 4414 gene show no color/b-gal production and therefore, had no interaction occur. The N50 and N75 cultures appear to be the most consistently dark out of all others; however, C25 does have a similar appearance to N25 and N50 indicating a similar production of b-gal and experience of interaction. Between N25 and N50, the consistent-dark color on the plates could potentially reflect an area among these regions responsible for the interaction. As for C25, a similar appearance to N25 and N50 could implicate the region as playing a role in the interaction.

Gaucher disease (GD) is an autosomal recessive inborn error in the pathway of sphingolipid catabolism. Biochemically, this disease is characterized by a deficiency of lysosomal β-glucosidase (glucocerebrosidase GCase, E.C.3.2.1.45) enzyme due to the mutation of GBA gene [1]. The natural substrate of this lysosomal enzyme is glucocerebroside (also called glycosylceramide) mainly present on the cytoplasmic face of cellular membranes and on the cell surface. Lysosomal β-glucosidases play a key role in recycling of this substrate by degradation of glucospingolipid from membranes of apoptatic white blood cells and senescent red blood cells. Genetic mutations of GBA gene affect the enzyme`s catalytic activity and stability and results in the storage

Mutations in the NAGA gene interfere with the ability of the alpha-N-acetylgalactosaminidase enzyme to perform its role in breaking down glycoproteins and glycolipids. These substances accumulate

As a reducing sugar, fructose reacts with protein molecules to form toxic advanced glycation end-products (AGEs) to a much greater extent than other sugars, which appears to contribute not only to the aging process but also play a role in the pathogenesis of diabetic complications in diabetic patients such as nephropathy, retinopathy, neuropathy and others. Supplementing the diet of healthy male volunteers with 3g of fructose per kg of body weight per day resulted in insulin resistance developing in as little as six days. A study carried out in non-diabetic rats fed a diet containing 68% carbohydrate, provided as fructose, shows that almost all retinas from the rats showed pathologic changes that were histologically indistinguishable from diabetic retinopathy. [1]

Gaucher’s disease (GD) is the most common lysosome storage disease in the world. There are three types of Gaucher’s. All types except type 1 are neuropathic form. Type 2 specifically is the most lethal and Type 3 neurological symptoms are need of the most support. Type 1 GD, can be observed in an individual as early as infancy into adulthood. The disease causes symptoms in skeletal, lungs, skin, eyes, lymphatic, blood and visceral organs. The drug Eliglustat is an agent that is used to treat type I Gaucher disease and Fabry’s disease. It is used with the method substrate replacement therapy (SRT) and it is used when enzyme replacement therapy (ERT) is not an option. The drug itself treat’s milder cases of the disease and is used more as a method

HS that contains -GlcA-GlcNS6S-, -GlcA2S-GlcNS- and -GlcA-GlcNS3S- is susceptible for heparanase cleavage17. Heparanase cleaves the bond between non-sulfated glucuronic acid and glucosamine carrying an N-sulfo or both N-sulfo and O-sulfo groups. In addition, heparanase recognizes glucosamine residues that contain N-sulfo and O-sulfo groups at +1 residue of the cleavage site. If the O-sulfation is not present, heparanase recognizes GluA2S located at +/-2 residues of the cleavage site17. In addition, heparanase has two cleavage modes; consecutive cleavage and gapped cleavage. The first step in both modes is similar in which heparanase cleaves the nonreducing trisaccharide end16. In the second step of consecutive mode, the linkage between the fifth and sixth residues is cleaved. On the other hand, the linkage between the seventh and ninth residues is cleaved in the gapped mode16.

The phosphate groups that are formed after the metabolism of fructose are used in other productions for instance the production of ATP. The aldolase B enzyme is found on chromosome 9. This intolerance can be inherited if both parents carry the gene but it would still only be a slim chance of actually getting the intolerance but that is how it happens. It’s estimated that it happens to about one in twenty thousand people. If diagnosed with this intolerance, a fructose free diet would be beneficial in follow. The symptoms are consistent with the diagnosis as well as the effects of what would happen if the patient is lacking the aldolase b enzyme.