Protein Chemistry Labratory
Texas A&M University
Department of Biochemistry
    & Biophysics,  Rooms 440-442
300 Olsen Blvd.
TAMU 2128
College Station, TX  77843-2128

    Directions to the PCL

Protein Chemistry Labratory
Texas A&M University
Department of Biochemistry
    & Biophysics,  Rooms 440-442
300 Olsen Blvd.
TAMU 2128
College Station, TX  77843-2128

    Directions to the PCL

PCL Links


Director
Larry Dangott
ljdangott@tamu.edu
Office phone: 979-845-2965
Lab phone: 979-845-2433
Fax: 979-845-8015


Director
Larry Dangott
ljdangott@tamu.edu
Office phone: 979-845-2965
Lab phone: 979-845-2433
Fax: 979-845-8015

Workshops

The Protein Chemistry Lab has successfully completed two 2D workshops in June with a total of 15 participants!  For more information future workshops please contact Larry by e-mail or phone at 979-845-2965.

Congratulations Pilar!

Our undergraduate student, Pilar Roper-Foo won a 2nd Place prize in the 12th Annual Student Research competitition.

 

Our undergraduate student, Pilar Roper-Foo won a 2nd Place prize in the 12th Annual Student Research competitition.

 

Myosin Heavy Chain Isoforms Separated with Electrophoresis

Myosin Heavy Chain (MHC) isoforms can be separated using acrylamide gels made with glycerol (Talmadge & Roy (1993), Blough et al (1996) and Reiser and Kline (1998). In collaboration with scientists at the University of Michigan Medical Center in Ann Arbor, the PCL has separated MHC isoforms in rat Soleus and Extensor digitalis longus muscle according to the procedure outlined by Reiser (1998). This procedure is now being applied to experimental samples provided by Dr. Melissa Melvin, the Department of Surgery.

 
             Sol                        EDL

 

Dr. Melvin is growing functional muscle in vivo in Dr. David Brown's Tissue Engineering laboratory at the University of Michigan Medical Center. The lab has succeeded in developing functional tissue-engineered skeletal muscle in rats, with its own blood vessel and nerve supply. The current goal of the research is to identify the mechanisms involved in innervating the new muscles with various nerves, as a means to maximize force and endurance for specific needs. Engineered muscles would be widely beneficial to patients with congenital or acquired muscle loss and/or paralysis.

If you are interested in this procedure, please contact the PCL.


References:

Talmadge, R.J. and R.R. Roy (1993) Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J. Appl. Physiol. 75, 2337-2340.

Blough, E.R, Rennie, E.R., Zhang, F. And P.J. Reiser (1996) Enhanced electrophoretic separation and resolution of myosin heavy chanis in mammalian skeletal muscles. Anal. Biochem. 233, 31-35.

Reiser, P.J and W.O. Kline (1998) Electrophoretic separation and quantiatin of cardiac myosin heavy chain isoforms in eight mammalian species. J. Appl. Physiol. 43, 1048-1053.

Myosin Heavy Chain (MHC) isoforms can be separated using acrylamide gels made with glycerol (Talmadge & Roy (1993), Blough et al (1996) and Reiser and Kline (1998). In collaboration with scientists at the University of Michigan Medical Center in Ann Arbor, the PCL has separated MHC isoforms in rat Soleus and Extensor digitalis longus muscle according to the procedure outlined by Reiser (1998). This procedure is now being applied to experimental samples provided by Dr. Melissa Melvin, the Department of Surgery.

 
             Sol                        EDL

 

Dr. Melvin is growing functional muscle in vivo in Dr. David Brown's Tissue Engineering laboratory at the University of Michigan Medical Center. The lab has succeeded in developing functional tissue-engineered skeletal muscle in rats, with its own blood vessel and nerve supply. The current goal of the research is to identify the mechanisms involved in innervating the new muscles with various nerves, as a means to maximize force and endurance for specific needs. Engineered muscles would be widely beneficial to patients with congenital or acquired muscle loss and/or paralysis.

If you are interested in this procedure, please contact the PCL.


References:

Talmadge, R.J. and R.R. Roy (1993) Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J. Appl. Physiol. 75, 2337-2340.

Blough, E.R, Rennie, E.R., Zhang, F. And P.J. Reiser (1996) Enhanced electrophoretic separation and resolution of myosin heavy chanis in mammalian skeletal muscles. Anal. Biochem. 233, 31-35.

Reiser, P.J and W.O. Kline (1998) Electrophoretic separation and quantiatin of cardiac myosin heavy chain isoforms in eight mammalian species. J. Appl. Physiol. 43, 1048-1053.

PCL is Back to Work - Wednesday, June 25, 2008

The Protein Chemistry Lab has successfully completed our first DIGE training workshop.  We had a great week working with five local TAMU scientists.  One student commented that the workshop was "more than I expected.  Excellent overall."  Please check back for more details on our next DIGE workshop..

The Protein Chemistry Lab has successfully completed our first DIGE training workshop.  We had a great week working with five local TAMU scientists.  One student commented that the workshop was "more than I expected.  Excellent overall."  Please check back for more details on our next DIGE workshop..

PCL Services - Wednesday, May 07, 2008

Remember that we still offer full services for protein analysis including DIGE Differential Gel Electrophoresis for quantitative Expression Proteomic analysis. This technique will help you identify proteins of interest between samples of different treatments using DeCyder software from GE Healthcare. Come in and see what it can do for you!

Remember that we still offer full services for protein analysis including DIGE Differential Gel Electrophoresis for quantitative Expression Proteomic analysis. This technique will help you identify proteins of interest between samples of different treatments using DeCyder software from GE Healthcare. Come in and see what it can do for you!