Home
BIOC 311 Team Library Project
The details for this project are in the "Library Project"
Assignment in Canvas. The
class will collect materials to be used as references for the
course. As you gather your information try to evaluate the
source materials for ease of use, for amount of information,
and for the type of information. Note any problems that you
encounter.
Examples of ACCEPTABLE references include
- Primary Journal Articles
- Review Articles (e.g., Annual Review in Biochemistry)
- Methods in Enzymology
- Methods in Enzymatic Analysis
- Enzyme Handbook
- CRC Handbook of Biochemistry
- Books (NOT textbooks)
Examples of UNACCEPTABLE references include
- Web Sites (URL's are here today/gone tomorrow; also, sites are UNREGULATED)
- Dissertations/Theses (sometimes these can be used BUT I do NOT accept them for this course)
- Textbooks (information is too general and often out of date)
NOTE: DO NOT LIMIT YOUR LITERATURE SEARCH TO RECENT PUBLICATIONS
ONLY--some of the references needed were published in 1940's
to 1980's. ONLINE references are acceptable if you include all
the information listed below and an online ID.
Assignment due on Day 2 or 3
- Research topics will be assigned on the
first day of lab
- Each team in each lab section must
submit a document (Assignments in Canvas
that includes a summary and the COMPLETE references
for their assigned topic
- A complete reference contains these SIX items
- Author(s) [ALL of them if less than 5; if 5 or more, use first author followed by "et al."]
- Title of journal article/book chapter
- Name of journal/book
- Issue # of journal/book publisher
- Page #'s
- Year of publication
- I will upload the references collected
by ALL teams into BIOC 311 Files in Canvas
NOTE: you will have to look up the reference to make sure
it's applicable and to get specific information for your paper
Project
Our lab has obtained a strain of E. coli that is
reportedly transformed with a plasmid to express murine adenosine
deaminase (ADA). Your assignment is to characterize the deaminase
protein produced in these cells to compare the findings with
the native deaminase extracted from mouse tissue.
Before beginning the project the following information is required:
Background information:
What reaction does adenosine deaminase catalyze?
What are the physiological functions associated with this reaction?
What mammalian tissues contain adenosine deaminase? What about
non-mammals?
What problems result if ADA is not present? What if
ADA is present in excess?
Known physical characteristics of adenosine deaminase
(especially from mouse and E. coli):
molecular mass
isoelectric point (pI)
Km's for adenosine and 2'-deoxyadenosine
Ki's and type of inhibition of common inhibitors (especially N6-methyladenosine or methylaminopurine)
Assay for adenosine deaminase (report at least two different
methods; one of these must be a spectrophotometric assay):
reaction - basis of the assay (what is being monitored?)
buffer conditions
substrate concentrations
pH
spectrophotometric assay
- extinction coefficient at 265 nm for
the conversion
of adenosine to inosine by ADA
- extinction coefficient at 235
nm for the conversion of adenosine
to inosine by ADA
Purification schemes and conditions that have been used for:
E. coli adenosine deaminase
- What buffer conditions were used?
- What gradients were used on ion exchange columns?
- What was the specific activity of the final preparation
mouse adenosine deaminase
- What buffer conditions were used?
- What gradients were used on ion exchange columns?
- What was the specific activity of the final preparation
Copyright, Acknowledgements,
and Intended Use
Created by B. Beason (bbeason@rice.edu), Rice University, 11 June 1999
Updated 22 August 2016