Your  Account:

Betsy A. Read

Betsy A. Read

Betsy A. Read profile picture
Professor CSTEM Biology
(760) 750-4129 Science Hall 2 131

About Betsy A. Read

Dr. Read's area of specialization is Molecular Cell Biology. She is the founder/initiator of the Biotechnology program at CSUSM and teaches core courses for the major. Currently, she is working on the molecular mechanisms of calcification and coccolithogenesis in the marine algae, Emiliania huxleyi, and her general research interests lie in the area of functional genomics. Prior to her arrival at CSUSM in 1993, she was a Postdoctoral Fellow in the Microbiology Department at The Ohio State University.


Wahlund, T.M. , X. Zhang, and B.A. Read. 2004. EST Expression Profiles from Calcifying and Non-Calcifying Cultures of Emiliania huxleyi . Journal of Micropaleontology. Accepted April, 2004. Publication Date, Special Issue, Fall 2004.

Wahlund, T.M., Hadaegh, A.R., Clark, R*., Nguyen, B*., Fanelli, M*., and B.A. Read. Analysis of Expressed Sequence Tags from Calcifying Cells of the Marine Coccolithophorid, Emiliania huxleyi. Journal of Marine Biotechnology, In Press, March 2004.

 Laguna, R*., J. Romo*, B.A. Read, and T.M. Wahlund. 2001. Induction of Phase Variation Events in the Life Cycle of the Marine Coccolithophore Emilania huxleyi. Appl. Environ. Microbiol. 67(9):3824-3831.

Read, B.A. & F.R. Tabita.  1994. High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eucaryotic marine algae and properties of recombinant cyanobacterial rubisco containing "algal" residue modifications. Arch. of Biochem. and Biophys., 312(l), 210-218.

Read, B.A. & F.R. Tabita. 1992. A hybrid ribulose-bisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor. Biochemistry, 31, 5553-5560.

Read, B.A. & F.R. Tabita. 1992. Amino acid substitutions in the small subunit of ribulse- 1, 5 -bisphosphate carboxylase/oxygenase that influence the catalytic activity of the holoenzyme. Biochemistry, 30, 519525.

[ back to top ]