HDTenEightyP/NetNews huggingface dataset:
From: bsh@MED.PITT.EDU (Basavaraju Shankarappa)
Newsgroups: bionet.molbio.methds-reagnts
Subject: Re: dye-term removal after cycle seq rxns
Date: 10 Sep 92 14:52:34 GMT
Distribution: bionet

> Hello fellow netters,
> 	I've a question regarding clean-up of dye-terminator cycle sequencing
> reactions.  Specificaly, does anybody out there have any nifty, simple, 
> cheap protocols for using home-made spun columns for this step?  I've used
> G-50 packed Eppies spun in a Speed-Vac before to remove unicoprorated counts
> after probe making, but I'm uncertain if this method is going to remove 
> sufficient dye-terminators to give good clean sequence.  I'd rather not 
> waste reactions to find out if somebody already knows the answer.
> 	Any helpful suggestions would be most welcome,
> 		Cheers,
> 			Jeremy
> =-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=
> Dr. Jeremy Weinman				Email:	jjw@rsbs1.anu.edu.au	
> Plant Microbe Interaction Group			Phone:	61 6 2495051
> Research School of Biological Sciences		Fax:	61 6 2490754
> Australian National University			Snail:	PO Box 475, Canberra, 
> 							ACT 2601, AUSTRALIA
> 

Yes, I have been doing what you have desribed above, using eppies.  I use
about 300 ul (not more) of the G-50 gel in a 500 ul eppie that has been 
pierced with a 25 guaze needle and poured with 1mm glass beads.  I treat
the glass beads with conc HCl (dont ask me why), neutralize, wash with 
TE and dispense about 10-25 ul per tube.  THen the tube is overlaid with
G-50 so that the total gel volume that is reatained in the tube is not
more than about 300 ul, spin in a table top centrifuge for 5 mins at about
1000 rpm to remove the fluid.  I add the 20 ul PCR reaction mix to the top
of the gel, rinse the PCR reaction tube with another 20 ul of TE and add it
to the gel.  Now I spin the double deckered tubes in the table top, but at
a speed that is about 500 rpm more than the previous spin.  The eluant that
is collected is now precipitated with atleast 3 volumes of ethanol (I have
seen that you lose lot of DNA if you do not add excess ethanol).  Incidentally
I make sephadex in 0.3M sodium acetate so that I eliminate the bother of 
adding the salt after chromatography.  
I realize there are many places you can alter the above procedure.  But the
above procedure has been working for me.  Also if the reaction worked and 
you were able to get all the DNA through the column, I invariably see a
pellet after ethanol ppt whenever the reaction worked well.  So this has been
a fairly rough guide.  
I hope there are other better procedures out there.  
Raj Shankarappa.
Univ of Pittsburgh
From: batc@ac.dal.ca
Newsgroups: bionet.molbio.methds-reagnts
Subject: Re: re ligation trouble
Date: 9 Sep 92 21:02:42 GMT
Distribution: bionet
Organization: Dalhousie University, Halifax, Nova Scotia, Canada

In article <1992Sep9.085708.17107@gserv1.dl.ac.uk>, skspoidn@susssys1.reading.ac.uk writes:
> re SphI ligations:
> 
> have you tried sacrificing a chicken under a full moon? :)
> 
> Seriously, 3 small suggestions, because 
> I have difficulty with 3' overhangers as well
> 
> 1) You don't mention if the alk phos treatment worked. I find that 3'
>  overhangs are much harder to dephos than 5' or even blunt.
> 
> 2) What is the composition of your ligase buffer? We recently changed 
> to Promega and were horrified to discover that the buffer as supplied
>  contains no condensation agents (usu glycerol or PEG), and that these
>  agents should be added by the user if neccessary. You could try upping 
> these components to max levels and see if that helps.
> 
> 3) Without wishing to appear arrogant, condescending or patronising,
>  have you ensured that your ratio of insert to vector is appropriate?
> 
> Hope this helps,
> 
> Mike Poidinger
> Dept of Microbiology
> University of Reading
From: rbonfigl@waite.adelaide.edu.au (Rod Bonfiglioli)
Newsgroups: bionet.molbio.methds-reagnts
Subject: graft pcr, help needed********
Summary: ;looking for protocols
Keywords: graft pcr, help
Date: 15 Sep 92 06:19:51 GMT
Organization: The University of Adelaide, Waite Campus
NNTP-Posting-Host: schooner.waite.adelaide.edu.au
Faculty: Agricultural & Natural Resource Sciences

does anyone please have some information or protocols on "recombinant" or
"graft" pcr.  the fragments i am trying to join are 100-200nts long and overlap
by 60-100nts.  any info or expertise that anyone could offer here would be
greatly appreciated,


thanx in advance

rod bonfiglioli,
email rbonfigl@schooner.waite.adelaide.edu.au
From: daryl@RT2.MENZIES.SU.EDU.AU (Daryl Webb)
Newsgroups: bionet.molbio.methds-reagnts
Subject: PCR1 and pSI 4001
Date: 15 Sep 92 07:29:43 GMT
Distribution: bionet

Hi troops, as part of an U/grad cloning project we are using _e.coli_ PCR1
strain and pSI 4001 as the vector.  We are also using Glutamate selection.
I'm having trouble locating useful references to these beasties.  If any one
out there knows where I can find a genotype,etc for PCR1, a map for pSI 4001
and a summary of the underlying principles of Glutamate selection please let
me know.

--  (P.S  yes Rod it's one of K.C's) 
                                                     |      |
  Daryl Webb  (daryl@menzies.su.edu.au)               \    / 
  Menzies School of Health Research                    \__/   
  P.O. Box 41096                                        ||   <<
  Casuarina N.T. 0811       _-*_|\---------------------- *  <<
  Australia                /      \                     ||   <<
  Voice : 61_89_228196     \_.--._/                    /||\ 
  Fax   : 61_89_275187           v                    * || o
                                                     /  ||  \
From: fish@LINDA.LLNL.GOV (chris)
Newsgroups: bionet.molbio.methds-reagnts
Subject: Re: lambda won't cut
Date: 10 Sep 92 21:19:18 GMT
Distribution: bionet


In article <9209091448.AA23264@server.uga.edu>, mcgraw%gandal.dnet@SERVER.UGA.EDU writes:
> A colleague provided us with some lambda clone DNAs "purified" from plate
> lysates.  They won't cut with EcoR1.  We tried further purification with
> additional phenol/chloroform extractions.  The uncut DNA looks good on a
> gel, and the OD's are good.  The inserts should cut out with EcoR1 based on
> the way the library was made (R1 linkers).
> 
> What do you suggest?


The problem could very well be intrinsic to the clones themselves.  That is, 
one (or both) EcoRI site(s) may have been damaged during the cloning step.  When 
you say EcoRI linkers were used, are these linkers the old-fashioned type? i.e., 
the kind where you have to digest with large excess of EcoRI to generate sticky
ends?  My experience with cDNAs from libraries made in this way is that a
substantial number of clones may have inserts that cannot be liberated due to
damaged RE sites.  Sometimes this even happens with cDNAs made using linkers
that do not have to be digested.  The best way to get around this problem (I 
assume you're subcloning the insert) is to use PCR to amplify the insert
with primers flanking the cloning site.

Chris Amemiya
Human Genome Center
Lawrence Livermore National Laboratory
Newsgroups: bionet.molbio.methds-reagnts
From: ALSOBROOK@biomed.med.yale.edu (John Alsobrook)
Subject: Re: PCR enhancers
Organization: Yale University
Date: Tue, 15 Sep 1992 17:30:48 GMT
X-News-Reader: VMS NEWS 1.20

In <9209101632.AA03158@anolis.bnr.usu.edu> thsiao@ANOLIS.BNR.USU.EDU writes:

> Dear Netters,
> 
> I am interested in the use of PCR enhancers.  I would like to know if any one
> has experience with the use of Stratagene's Perfect Match Polymerase Enhancer.
> Is this a single-stranded DNA binding protein?  What is the difference with
> USB's single-stranded DNA binding protein or GP 32?  How effective are these
> products in getting better PCR yields?  Any suggestion and tips will be
> appreciated.
> 
>    +---------------Ting H. Hsiao ---------------+
>    | Dept. of Biology, Utah State University    |
>    | Logan, UT 84322-5303, U.S.A.               |
>    | PHONE: (801) 750-2549; FAX: (801) 750-1575 |
>    | E-MAIL: thsiao@anolis.bnr.usu.edu          |
>    +--------------------------------------------+


An issue of Biotechniques (I think, not absolutely sure) a couple of years ago
revealed that Stratagene's Perfect Match is actually a 5x10E-5 M solution of
tetra-methyl-ammonium chloride.

****************************************************************************
*                                       | "Giving money and power to the   *
* John Alsobrook                        |    government is like giving     *
* Child Study Center                    |     whiskey and car keys to      *
* Yale University School of Medicine    |  teenage boys." - P.J. O'Rourke  *
*--------------------------------------------------------------------------*
*               internet:alsobrook@biomed.med.yale.edu                     *
*--------------------------------------------------------------------------*
...and, of course, nothing I ever say is officially sanctioned by Yale...
From: gat44@iastate.edu (Gabriel Trueba)
Newsgroups: bionet.molbio.methds-reagnts
Subject: Lambda EMBL
Date: 15 Sep 92 02:39:03 GMT
Distribution: bionet
Organization: Iowa State University, Ames, IA

Dear Netters

Does anybody know why E.coli strain 1090r-(RecA+) is not 
used for lambda EMBL libraries?. I am aware of the fact
that P2 lysogens are the best.

gat44@iastate.edu
From: KNECHT@UCONNVM.UCONN.EDU (Dave Knecht)
Newsgroups: bionet.molbio.methds-reagnts
Subject: RE-use of Hyb solutions
Date: 6 Sep 92 05:16:10 GMT
Distribution: bionet

We routinely re-use random pprimed probe hyb solutions.  We store at -20 and bo
il for 10 minutes before adding to the filter.  We have used some up to 10x but
 then the signal does drop.
From: dreyfuss@hmivax.humgen.upenn.edu
Newsgroups: bionet.molbio.methds-reagnts
Subject: TYE Medium?
Date: 11 Sep 92 22:15:00 GMT
Organization: HHMI/Human Genetics, Univ of Pa.

Hello--

Does anyone out there know about the composition of TYE medium for growing
E.coli TG1 cells?

Thanks,
Jeong-Kook Kim
Howard Hughes Medical Institute/University of Pennsylvania
Internet:  dreyfuss@hmivax.humgen.upenn.edu
(215)898-0172
From: Greenleaf@bchm.biochem.duke.edu (Andrea Skantar)
Newsgroups: bionet.molbio.methds-reagnts
Subject: Acidic polyacrylamide gels
Date: 8 Sep 92 15:04:26 GMT
Distribution: bionet
Organization: Duke University Biochemistry Dept.

I am studying protein-protein interactions as described in the post of 
Cornelius Krasel recently.  In particular, I have tried the so-called
"far-Western" blot technique, where you use labeled protein as a probe
instead of antibody.  So far I have not seen anything and I have recently
learned that the protein I'm trying to detect has two subunits, one with
a pI around neutral and the other at pI=10.4.  So I'm not sure that this
protein has been entering the gels I've been running in Tris-glycine at 
pH=8.  Does anybody have any info on native acidic polyacrylamide gels?
We don't have isoelectric focussing equipment.  Any advice from people who
work on histones or other basic proteins?  I'd appreciate any input.  

Thanks,

Andrea
From: djt2@po.CWRU.Edu (Dennis J. Templeton)
Newsgroups: bionet.molbio.methds-reagnts
Subject: Re: UV Shadowing
Date: 11 Sep 1992 17:48:41 GMT
Organization: Case Western Reserve University, Cleveland, OH (USA)
Reply-To: djt2@po.CWRU.Edu (Dennis J. Templeton)
NNTP-Posting-Host: thor.ins.cwru.edu


In a previous article, SMITH_DENNIS_P@LILLY.COM ("DENNIS P. SMITH") says:

>Need advice of how to take photograph of an oligonucleotides using UV
>shadowing. Can anyone suggest a reliable technique? Thanks DPSMITH
>

Put your gel on a piece of Saran Wrap, and lay it atop a fluorescing
substrate (More on this below).  Then use a hand illuminator to shine
through the gel, and detect dark spots on the otherwise bright background.

Finding the right fluorescing plate is sometimes tricky.  What always works
is the glass cellulose TLC plates that are marked "with fluorescence
indicator"; maybe the plastic plates or the silica TLC plates work too.  We
use instead an intensifying screen, but it turns out that many screens
don't work (they don't fluoresce brightly)... we tried about 15 and only
one (an old one with lots of cracks) works for us.  

If you use the glass fluorescing plates, you can put the gel on a
transilluminator, cover with Saran, then place the plate over and view from
the top, i.e. the back of the plate.

good luck,

dennis
From: DMEIER@mis.mcw.edu
Newsgroups: bionet.molbio.methds-reagnts
Subject: custom made cDNA libraries
Date: 8 Sep 92 22:09:13 GMT
Distribution: bionet
Organization: Medical College of Wisconsin (Milwaukee, WI)

Hello to the net,
  Does anyone have and experience and/or comments on commercial sources of 
custom-made cDNA libraries?  Are some companies more reliable than others? 
Has company management sat through Dr. Deming's lectures, or do they have 
the attitude "So you're having problems with our product?  No one else 
does.  Do you need a brain transplant?"  I actually had an experience like 
that with an antibody supplier.  If there is a FAQ on this question, how 
would I locate it?
Thanks much.

Dan Meier
MCW, Milwaukee
Newsgroups: bionet.molbio.methds-reagnts
From: horton@molbio.cbs.umn.edu (Robert Horton)
Subject: Re: AMMONIA CLEAVAGE FROM PROTEINS
Organization: University of Minnesota
X-Newsreader: Tin 1.1 PL5
Distribution: bionet
Date: Mon, 14 Sep 1992 18:19:09 GMT

BECKERM@SIMSC.EARN (BECKERM@MSCSI.BITNET) wrote:

: I'M LOOKING FOR REFERENCES OF AMMONIA CLEAVAGE FROM PROTEINS...
                                ^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^
Do you mean deamidation, like converting asparagine to aspartic acid?
If so, you might want to look at

	Robinson, AB (1979) "Molecular clocks, molecular profiles, and 
optimum diets: three approaches to the problem of aging." Mechanisms of
 Aging and Development 9:225-236.

	Robinson, AB and Robinson LR (1991) "Distribution of glutamine and
asparagine residues and their near neighbors in peptides and proteins" Proc.
Nat'l. Acad. Sci., USA (sorry, I have a preprint with no page numbers!)

	The basic tenet is that deamidation may be used in nature as a
"molecular clock" mechanism by which proteins age, and the deamidation 
rate is apparantly affected by primary sequence, so that proteins can  
evolve to "age" at different rates.

--
Bob Horton            /\ "Crash programs fail because of the theory that
U. of Minnesota, CBS  || with nine women pregnant you get a baby a month" 
1479 Gortner Ave.    /||\   -Werner von Braun.  Disclaimer:"Bob who?"
St. Paul, MN 55108    ^^   horton@molbio.cbs.umn.edu/(612) 624-3790
From: justman@husc10.harvard.edu (Craig Justman)
Newsgroups: bionet.molbio.methds-reagnts
Subject: N-ter labelling of proteins
Date: 14 Sep 92 21:38:13 GMT
Distribution: bionet.molbio.methds-reagnts
Organization: Harvard Arts and Sciences Computer Services, Cambridge, MA



i am interested in biotinylating a protein via NHS chemistry; i can get the
reaction to go, but no matter the stoichiometry of the reaction, i end up 
with a mixed population of multiply labelled protein (by IEF i can see
mono-labelled protein along with bis, tris... all the way up to 8 labels 
per molecule (8 lysines)).  i would like to label the protein in a more
controlled manner.

i have seen allusions in the current literature to label the n-terminus
specifically by controlling the pH of the reaction, but have found no 
references.  before i go re-inventing the wheel and trying to determine the
optimal pH (by wasting protein and reagent), i would like to know if anyone
has seen such a reference (or am i missing something obvious?)

thanks.
Newsgroups: bionet.molbio.methds-reagnts
From: danj@welchgate.welch.jhu.edu (Dan Jacobson x-8453)
Subject: Re:  Hgie II
Organization: Johns Hopkins Univ. Welch Medical Library
Date: Mon, 7 Sep 1992 16:27:35 GMT

A request was made for information about a restriction enzyme,

A quick wais search of Rebase yields the following:


<1>HgiEII
<2>
<3>Herpetosiphon giganteus Hpg24
<4>H. Reichenbach
<5>ACCNNNNNNGGT
<6>
<7>
<8>Kroger, M., Hobom, G., Schutte, H., Mayer, H. Eight new restriction endonucle
ases from Herpetosiphon giganteus - divergent evolution in a family of enzymes.
 Nucl. Acids Res. 12: 3127-3141 (1984)


You might want to contact the aothors for more information.

Dan
From: robert@arbo.microbiol.uwa.oz.au (Robert Coelen)
Newsgroups: bionet.molbio.methds-reagnts
Subject: re: Epstein Barr
Date: 8 Sep 1992 08:55:43 GMT
Organization: University of Western Australia
NNTP-Posting-Host: mve.microbiol.uwa.edu.au

In article <9209042327.AA25667@sol.UVic.CA> jdboer@SOL.UVIC.CA (Johan deBoer) writes:
>
>
>
>
>
>
>     Fellow moleculars,
>
>     We are considering some work with  the Epstein Barr virus, and have  a
>     few questions about it that we hope someone is able to answer.
>
>     1)   What is the proper (latin  I guess) species, genus, organism etc.
>          name for this virus?

Epstein-Barr virus is the proper name for this organism. In virology
we do not employ the genus/species concept with latin names and a common
name as a substitute


>
>     2)   The virus resides  in a cell line called MCUV5. What cell line is
>          this, where does it come from, what does the name mean?

I'll attempt to look that one up ! Anyone with ideas to go online to ATCC ?
>
>     3)   What are  the clinical  aspects, dangers,  risks, etc  associated
>          with working with EBV?
>
>
Epstein-Barr virus (EBV) is a herpes virus and is an aetiological agent of
glandular fever (infectious mononucleosis). The virus is also strongly 
implicated as having a causal relationship to African Burkitt's lymphoma
and to nasopharyngeal cancer (note other cofactors are generally present !)
The major route of transmission of EBV in young adults appears to be kissing
with exchange of saliva (not the kiss on the cheek variety !). Evidence from
cases on a submarine indicates that close contact (but not kissing) is not
sufficient to transmit the virus. Whilst the virus appears not to be very contagious,
one of the early cases of infectious mononucleosis attributed to EBV was in
a technician in a lab where they worked with it. Present day biohazard hoods
and good microbiological practices (gloves, alcohol wiping surfaces, etc) should
be sufficient to keep you free of EBV. One of the Klein's worked with EBV for a
lifetime and never seroconverted !

>     Any  comments, or pointers  to as where  the information  can be found
>     would be greatly appreciated.
>
>     Johan de Boer
>     jdboer@sol.uvic.ca
>     University of Victoria, BC

Robert Coelen
Department of Microbiology
robert@arbo.microbiol.uwa.edu.au
!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!
drop me an e-mail line if you are reading this (and therefore interested in virology
From: wmelchior@NTBTOX.NCTR.FDA.GOV ("Bill Melchior, NCTR/FDA")
Newsgroups: bionet.molbio.methds-reagnts
Subject: Re: Re: ASAP
Date: 9 Sep 92 18:56:19 GMT
Reply-To: wmelchior@NTDOC.NCTR.FDA.GOV
Distribution: bionet

>Yes, there really is an Artic shrimp alk. phos. [ASAP]
>....Even more suprising is that
>it really works.  Best part is that you can digest and SAP at the
                                             ^^^^^^^^^^^^^^
>same time.

Do you mean restriction digest and dephosphorylate simultaneously?
While typical restrictions are done near neutrality (pH 7.5 for the Maniatis
etal buffers), USB compares ASAP with calf intestinal AP at pH 9.6.
(But they do suggest pH 8 for the reaction -- why?)  Have you used ASAP with 
different restriction buffers?  Could you be specific about your conditions?

Thanks.
________________________________________________________________________________
The opinions stated are mine, not those of NCTR or its sponsoring organizations.

Bill Melchior                                ||   "You have lawyers the way
National Center for Toxicological Research   ||    other people have mice."
Jefferson, AR  72079                         ||
(501) 543-7206                               ||   -Kenneth Duncan, English
                                             ||    Health & Safety Executive,
WMELCHIOR@NTDOC.NCTR.FDA.GOV                 ||    to US regulators
From: READY@UTBC01.CM.UTEXAS.EDU
Newsgroups: bionet.molbio.methds-reagnts
Subject: Direct PCR of Lambda Libraries
Date: 14 Sep 92 13:09:21 GMT
Distribution: bionet

Dear Netters,

	I recall hearing or reading of a method for PCR of a desired poly-
nucleotide directly from a cDNA library in Lambda phage. The idea was that for
a more-or-less known sequence, one could take a few ul of the phage, strip
their coats and use the DNA directly in a PCR reaction. If anyone has a method
or can point me to the reference, I would be a very happy guy (my hair is
getting to thin for continued 32P use). If there is sufficient interest, I'll
post a summary of responses.

Thanks in advance,

Mike R.
    _______________________________________________________________________
   | Dr. Michael P. Ready                     | READY@UTBC01.CM.UTEXAS.EDU |
   | Clayton Foundation Biochemical Institute | Phone: (512)471-3625       |
   | University of Texas                      | FAX:   (512)471-8696       |
   | Austin, Texas 78737                      |                            |
   |__________________________________________|____________________________|
From: sbhattac@crc.ac.uk (Dr. Shoumo Bhattacharya B1 061)
Newsgroups: bionet.molbio.methds-reagnts
Subject: DNA methylation
Date: 14 Sep 92 16:34:23 GMT
Distribution: bionet
Original-To: methods@uk.ac.daresbury

This is a summary regarding my query on demethylating DNA in cell culture
using azacytidine.

The dose of azaC is between 1-10 uM, and cells are exposed to this for 
approx 24 hours.  One cell cycle in presence of the drug produces
hemimethylation, and further divisions result in double strand 
demethylation. 

A good reference is Razin A., Cedar H.  Microbiol. Rev.  1991, 451-458
Thanks  to those who replied.
Dr. Shoumo Bhattacharya				
MRC Molecular Medicine Group
Royal Postgraduate Medical School
Hammersmith Hospital, DuCane Road London W12 0NN
Newsgroups: bionet.molbio.methds-reagnts
Subject: Re: Acidic polyacrylamide gels
From: power@mbcf.stjude.org
Date: 11 Sep 92 10:45:14 -0600
Distribution: bionet
Organization: St. Jude Children's Research Hospital

In article <5175@news.duke.edu>, Greenleaf@bchm.biochem.duke.edu (Andrea Skantar) writes:
> I am studying protein-protein interactions as described in the post of 
> Cornelius Krasel recently.  In particular, I have tried the so-called
> "far-Western" blot technique, where you use labeled protein as a probe
> instead of antibody.  So far I have not seen anything and I have recently
> learned that the protein I'm trying to detect has two subunits, one with
> a pI around neutral and the other at pI=10.4.  So I'm not sure that this
> protein has been entering the gels I've been running in Tris-glycine at 
> pH=8.  Does anybody have any info on native acidic polyacrylamide gels?
> We don't have isoelectric focussing equipment.  Any advice from people who
> work on histones or other basic proteins?  I'd appreciate any input.  
> 
> Thanks,
> 
> Andrea


Re: Acidic polyacrylamide gels

Andrea,
I have recently been working on the matrix protein of human parainfluenza virus
type 1,  which is highly basic.  I had a considerable problem trying to get the
protein to enter a regular Laemmli PAGE-SDS gel (pH 8.8).  However,  by simply
making up the gel using Tris-Cl pH 7.4 instead of the regular pH 8.8 I was able
to get the protein to enter the gel and resolve at the anticipated size
relative to protein markers.  One word of caution,  you may need to increase
the concentration of the polyacrylamide,  as at this pH low mw proteins do not
resolve from the dye-front.  The protocol needs refinement but it may help you
get a handle on your problem.  Look out for a paper due out soon in Virology by
Power, U.F., Ryan, K.W.,  and Portner, A.,  entitled Sequence characterization
and expression of the matrix protein gene of human parainflueuza virus type 1.
Good luck.
Ultan Power
email: Power@mbcf.stjude.org
tel: (901)522-0466