•  
  •  
 

1st Student's Major

Chemistry and Geology

1st Student's College

Science, Engineering and Technology

Students' Professional Biography

Rehan Ahmed Malik was born and grew up in Karachi, Pakistan. In December 2000, he received a BSc. degree (major in Chemistry and minors in Microbiology and Biochemistry) from University of Karachi in Karachi, Pakistan. After his Graduation he moved to Mankato, Minnesota, USA for further studies. Now he has recently graduated from Minnesota State University, Mankato on May 14, 2005 with BS degree in Biochemistry and minor Computer and Information Sciences. He conducted an undergraduate research project on “Identification of Soybean Lipoxygenase products by GC-MS assay” in fall 2004 under the supervision of Dr. James Rife. He was awarded a grant for this research by URC. He participated in the URC conference and presented his research work in the form of PowerPoint presentation on April 26, 2005. Now he is willing to earn a PhD in neural sciences from a reputable University.

Mentor's Name

James Rife

Mentor's Email Address

james.rife@mnsu.edu

Mentor's Department

Chemistry and Geology

Mentor's College

Science, Engineering and Technology

Abstract

Lipoxygenases (LOXs) are enzymes which catalyze peroxidation of polyunsaturated fatty acids containing at least one cis, cis 1, 4-pentadiene moiety to form conjugated diene-hydroperoxides. Soybean seeds contain three LOX isoenzymes while at least five different isoenzymes are in the vegetative tissue. Lipoxygenases have been related to several functions i.e. plant growth, defense mechanisms against pathogens and pests, and lipid metabolism. Given the proposed roles of LOX isoenzymes and the presence of multiple LOX isoenzymes in soybean vegetative tissue, it is likely that individual isoenzymes play specific functions. Do the isoenzymes show differences in which products they form? The basic goal of this project was to develop a GC-MS assay to determine the product formed by soybean LOX, and determine the preferred products formed by the different isoenzymes. The complete characterization and comparison of products can give clues about the physiological roles of specific isoenzymes. In this research, linoleic acid and linolenic acid were used as substrates for LOX enzymes to analyze the primary reaction products of LOX in order to see which end of the 1, 4-pentadiene section is used in the reaction. The peroxidation of linoleic acid can take place either at Carbon atom 9 or the carbon atom 13 to form 9 hydroperoxylinoleic acid (9-HPOD) and 13-hydroperoxylinoleic acid (13 HPOD), respectively. Other reactants such as linolenic acid, which has three double bonds, can yield even more products. A GC-MS assay was developed and implemented for analysis of reaction products of LOX.

Creative Commons License

Creative Commons Attribution-Noncommercial 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License

Included in

Biochemistry Commons

Share

COinS
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.