which enzyme is responsible for converting Xgal to the blue product?
458712
Beta-galactosidase :o)
760435
You are looking at a displacement reaction, in which the more reactive metal (Cu) is displacing the less reactive metal (Ag) from its salt solution (AgNO3).\nCu (s) + 2AgNO3 (aq) --> 2Ag (s) + Cu(NO3)2 (aq)\n\nHope this helps. :)
792939
Glycogen phosphorylase uses phosphate instead of water to break down glycogen. Glycogen phosphorylase manages to use phosphate to catalyze glycogen breakdown by employing the coenzyme pyridoxal phosphate (PLP). This coenzyme forms a Schiff base intermediate with a lysine residue of the enzyme (see HERE). The 5' phosphate of PLP act as a proton donor and then as a proton acceptor (acid-base catalyst). Orthophosphate acts to donate a proton to carbon 4 of the glycogen chain and simultaneously acquire a proton from PLP. The carbonium ion thus created is attacked by orthophosphate to form alpha-glucose-1-phosphate. The mechanism can be seen HERE.
89543
r methyl viologen \n\nwow..this was a hard one\n\nIt appears to be used in Genome research.
840983
http://www.amano-enzyme.co.jp/english/productuse/others.html
748670
If the reaction goes to fast, i.e.the blue colour appears instantly, you can slow it down by adding more thiosulfate to the solution.\n\nI hope that helped, because otherwise the meaning of your question wasn't very clear to me.
219857
e gluconeogenesis (or b or c my brother guessed this)
856520
The first of the two key enzymes is unique to the ED pathway, 6-phosphogluconate dehydratase (Edd), which catalyzes a dehydration of 6-phosphogluconate to form KDPG. The second enzyme of the ED pathway, KDPG aldolase (Eda), catalyzes an aldol cleavage of KDPG to form pyruvate and glyceraldehyde-3-phosphate. The triose phosphate intermediate is further metabolized by the glycolytic pathway and provides energy via substrate-level phosphorylation.
958445
http://en.wikipedia.org/wiki/Glycolysis\n\nJust scroll down and look at reaction number 8 for the mechanism.
1088386
enzyme catalysis, defense, transport, support, motion, regulation, and storage.
840358
When you first add the bromothymol blue to your acidic solution, it will give a bright yellow color to the solution.\nWhen you titrate with NaOH, the endpoint will be a color change to Blue.
654853
Use a Bradford assay for protein. This uses a dye which goes from red to blue when it binds to proteins, and the colour change and hence the amount of protein present cana be assessed spectrophotometrically. This is a cheap, sensitive method and will give you a quantitative answer (providing you calibrate your spectrophotometer first using a standard curve produced with solutions of different known protein concentrations). This link will tell you more about the exact method.\n\nhttp://www-class.unl.edu/biochem/protein_assay/bradford_assay.htm
47201
2,6-DIDEOXY-BETA-D-GALACTOSE (DDL)
847602
Adenosine TriPhospahte (ATP) and NADH2\n\nIn response to answer above: GTP is only created from tyrosine-kinase reactors and is not part of the krebs cycle
252717
Plants store glucose as the polysaccharide starch. Starch can be separated into two fractions--amylose and amylopectin. Natural starches are mixtures of amylose (10-20%) and amylopectin (80-90%).\n\nAmylose in starch is responsible for the formation of a deep blue color in the presence of iodine. The iodine molecule slips inside of the amylose coil.\n\nIodine is not very soluble in water, therefore the iodine reagent is made by dissolving iodine in water in the presence of potassium iodide. This makes a linear triiodide ion complex with is soluble. The triiodide ion ion slips into the coil of the starch causing an intense blue-black color.
385735
The molecular mass of p-nitrophenylphosphatase is 33 kDa.
573178
http://www.dogpile.com/info.dogpl/search/web/%252527Utilization%252Bof%252Bstarches(sago)in%252Bthe%252Bproduction%252Bof%252Bbioethanol%252527/1/-/1/-/-/-/1/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/-/417/top/-/-/-/0