Posted: August 19th, 2015

Inhibitors of transglutaminase.

There 11 results see below. Look to the result carefully and explain it.
in some figures the comments are incorrect so write your discussion according to the result itself.
The main aims of the project are to partial purify TG2 from gpl, develop TG2 enzyme assay by using biotin cadaverine that utilized to determine the activity of TG2 inhibitors. Develop florescence assay that utilized to detect the inhibition activity of TG2. And also develop an electrophoretic assay for TG2 deamidation activity to show the inhibition by standard TG2, inhibitors such as polyamines, Z-DON, R283, EDTA and ca++.
1- 45 academic references from pubmed or sciencedirect (do not use any review articles). Reference should be related to the information because I bought some paper and references were not related. (So be aware about that).
2- Recent references from 2004 until now. (Use Havard style).
3- Plagiarism 0%.
4- Firstly, you should write introduction about the project.
5- You should link between all the assays by writing in the begging of each assay, for example the TG2 assay does not work that is why we are moving to the ammonia assay. ( write that in academic way).
6- Secondly, in Transglutaminase 2 assay there are two columns the first one about casein peptides you should discuss that and explain the inhibition (linear response). Which one produce more inhibition and no inhibition.
The second column is about DMSO you should discuss the relationship and the inhibition. (Please look for examples and do the same).

7- Thirdly, in ammonia assay you should discuss about the 4 graphs and explain the linear relationship between them.
8- In Fluorescence assay you should write in the begging the ammonia assay does not work that is why fluorescence assay was performed write it by academic way. And do the same with two firs assays.
In fluorescence assay you should discuss the background was high (control) and compare the all polyamines against the control.

9- Finally, in nondenaturing gel, firstly you should write about the natural deamidation (chemical deamidation) and contrast that with enzyme catalyze deamidation.
Secondly, you should write about why the storage protein is deamidated and give good visual.
In figure 8 you should discuss about the well (H) and (I) deamidation, and ather wells no deamidation.
In figure 9 you should discuss about the inhibitors prevent deamidation.
In figure 10 you should discuss about the well (F) and (G) why they do not get on the gel you need to talk about the molecular weight of β-crystaline and α-crystaline.
And in wells (B) and (C) the elafin protein does not appear in the gel you should discuss that.
You must support all the information above with references.

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