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To Session Abstracts Program Abstracts A-7. Information, Computing & Communications Index to Session Abstracts Division, Engineering & Technology Division and Social & Behavioral Sciences Division Saturday, April 5, 1997 Engineering, Social Science, Technology, Please see Author Index on page 61 and their Applications-37 to locate first authors of abstracts. 01:30PM Saturday, April 5, 1997 Olscamp Hall Room 217 Session Title-Page Number John K. Estell - Presiding Poster Sessions Earth & Space Sciences Division and Education Various Divisions-8 Division Education/Earth Science Education-36 Biological Sciences Division 09:00AM Saturday, April 5, 1997 Lake Erie Fish Biology-21 Olscamp Hall Room 217 09:00AM Saturday, April 5, 1997 Robert F. Mauldin - Presiding Olscamp Hall Room 221 Fred L. Snyder - Presiding General Geology-39 09:15AM Saturday, April 5, 1997 Lake Erie Ecosystem Status and Future-22 Olscamp Hall Room 213 01:30PM Saturday, April 5, 1997 Ann F.H. Graetsch Harris - Presiding Olscamp Hall Room 221 Mapping Tools & Quaternary Geology-40 Lauren Lambert - Presiding 02:00PM Saturday, April 5, 1997 Olscamp Hall Room 213 Plant Systematics & History of Botany-23 Yu Zhou - Presiding 09:00AM Saturday, April 5, 1997 Olscamp Hall Room 206 General Geography-41 Allison W. Cusick - Presiding 10:00AM Saturday, April 5, 1997 Olscamp Hall Room 215 Plant Biology-24 Joseph G. Spinelli - Presiding 02:00PM Saturday, April 5, 1997 Olscamp Hall Room 206 A Collective Look Ahead at Helen J. Michaels - Presiding Ohio's Future Geography-41 02:00PM Saturday, April 5, 1997 Plant Ecology-26 Olscamp Hall Room 215 09:00AM Saturday, April 5, 1997 Henry Moon - Presiding Olscamp Hall Room 224 Brent G. DeMars - Presiding Medical Sciences & Health Technologies Division Aquatic Ecology-27 Blood Pressure/Hypertension/Lung Ventilation-42 02:15PM Saturday, April 5, 1997 09:00AM Saturday, April 5, 1997 Olscamp Hall Room 224 Olscamp Hall Room 225 Rex L. Lowe - Presiding Judy Adams - Presiding Microbial Biology and Phycology-28 Hormones & Metabolism-43 09:00AM Saturday, April 5, 1997 01:30PM Saturday, April 5, 1997 Olscamp Hall Room 220 Olscamp Hall Room 225 Susan Carty - Presiding Steve Channel - Presiding Ecology-29 Physiological Control Mechanisms-44 01:30PM Saturday, April 5, 1997 09:00AM Saturday, April 5, 1997 Olscamp Hall Room 220 Olscamp Hall Room 227 Arthur L. Vorhies - Presiding Lee A. Meserve - Presiding Molecular Biology-31 Genetics & Molecular Biology-46 01:30PM Saturday, April 5, 1997 01:30PM Saturday, April 5, 1997 Olscamp Hall Room 229 Olscamp Hall Room 227 Dean Fraga - Presiding R. C. Woodruff - Presiding Biochemistry & Parasitology-33 Pre-College Session 03:45PM Saturday, April 5, 1997 Pre-College Students-Morning-47 Olscamp Hall Room 227 09:00AM Saturday, April 5, 1997 Rebecca R. McRenna - Presiding Olscamp Hall Room 203 James C. Brown - Presiding Environmental Sciences & Resource Management Division Pre-College Students-Afternoon-48 Environmental Science-34 02:30PM Saturday, April 5, 1997 09:30AM Saturday, April 5, 1997 Olscamp Hall Room 203 Olscamp Hall Room 226 Juanito S. Duran - Presiding Charles Bleckmann - Presiding Interdisciplinary Session - 61 Contaminant Removal-35 02:00-04:00 PM Saturday, April 5, 1997-49 03:45PM Saturday, April 5, 1997 Olscamp Hall Room 121 Olscamp Hall Room 226 Ayres D'Costa, Presiding Yung-Tse Hung - Presiding A-8. The Ohio Journal of Science Vol. 97(2) different serum proteins induced by sublethal doses of diazinon. Adult large POSTER SESSION mouth bass, Micropterus salmoides were exposed to 90LUJ/I, 180Lig/l, 270|ig/ I, 360u,g/l, and 450u,g/l of diazinon for 24 hr. Electrophorctic results showed a 9:00-10:00 AM significant increase in fraction 2 of the 270 and 450LUJ/I groups. In general, fraction 4 of all the diazinon exposed groups showed a significant decrease SATURDAY, APRIL 5,1997 compared to the control group. Fraction 5 of the 270u.g/l and fraction 6 of the 360 and 450u,g/l exposure groups showed significant decreases. A new serum OLSCAMP HALL protein, fraction 7, appeared in the 180Lig/l, 270LUJ/I and 360(ig/l exposure groups. Fraction 2 is considered to be a low-mobility protein which contains BOARD A INTERACTION OF HIGH MOBILITY GROUP 1 WITH TATA globulin. Increase in fraction 2 may be an immune response. Decrease in BINDING PROTEIN. D. DAS., W. SCOVELL. DEPARTMENT OF CHEMISTRY, BOWLING fractions 4, 5 and 6, which are high-mobility proteins and includes albumin, may GREEN STATE UNIVERSITY, BOWLING GREEN OH 43403. be related to necrosis in the hepatocytes of the liver. Formation of a new protein High Mobility Group (HMG) 1, an abundant, ubiquitous and highly may be attributed to cellular damages caused by this pesticide. conserved protein, plays a major role in transcription. HMG 1 consists of three domains, a N-terminal A-domain, central-B-domain and C-terminal-domain. BOARD E THE EFFECTS OF DIETARY LEAD AND CHOLESTEROL TBP, a sequence specific protein, recognizes the TATA element on the SUPPLEMENTATION UPON HEMOLYSIS IN THE SPRAGUE-DAWLEY eukaryotic promoter and initiates transcription. Ge and Roeder reported that RAT. BOYD R. RORABAUGH, LEE A. MESERVE, AND PAUL A. MOORE. DEPARTMENT OF HMG 1 binds to TATA binding protein both in solution and also on a DNA BIOLOGICAL SCIENCES, BOWLING GREEN STATE UNIVERSITY, BOWLING GREEN OH 43402. template. We confirmed the binding of HMG 1 to TATA binding protein in Hemolytic anemia has been observed in fish and in humans ex- solution. We are interested in mapping the domains of HMG 1 involved in TBP posed to lead. The goal of the present investigation was to test the hypothesis binding. The recombinant B domain of HMG 1 was expressed in E.coli, and that lead induces a cholesterol deficiency which is responsible for this hemolytic then isolated and purified. The TATA binding protein was expressed as a GST effect. Adult male Sprague-Dawley rats were divided into four groups. Group I fusion protein.The binding studies were done with reaction of GST-TBP fusion was the untreated control, group II was fed a 4% cholesterol supplemented diet, protein with HMG 1 or polypeptides containing its structural domains(HMG 1- group III was exposed to lead nitrate via the drinking water, and group IV was B-box). The HMG 1 or HMG 1-B-box protein was incubated with the reaction exposed to lead and the cholesterol supplemented diet. Blood samples were mixture containing the GST-TBP immobilized on the Glutathione Sepharose collected weekly for five weeks. Mean hematocrit, mean serum hemoglobin, beads. After washing off unbound proteins.the bound proteins were eluted off and mean cholesterol concentrations were not significantly different in lead the column and analyzed by SDS-PAGE and Western Blot. We report here the exposed animals. This indicated that acute lead exposure did not induce a interaction of HMG 1 B-box with GST-TBP using GST- capture experiments. cholesterol deficiency sufficient to cause hemolysis. The serum protein con- HMG 1-B-box binds to GST-TBP, with only residual binding to GST control. At centrations were significantly elevated in cholesterol supplemented rats irre- least the B-domain of HMG 1 is, in part, responsible for this interaction. spective of the addition of lead. However, the serum protein concentration of those animals exposed to both lead and cholesterol returned to normal after five BOARD B INTERACTION BETWEEN THE HIGH MOBILITY GROUP-1 weeks of exposure, while those exposed only to cholesterol remained elevated. PROTEIN, HMG-1, AND THE RETINOBLASTOMA PROTEIN, pRB. THOMAS This indicated the existence of a lead + cholesterol interaction that affected J. KOWSKI & WILLIAM M. SCOVELL. DEPARTMENT OF CHEMISTRY, BOWLING GREEN STATE serum protein (albumin) synthesis. UNIVERSITY, BOWLING GREEN OH 43403. The high mobility group-1 protein, HMG-1, is an abundant, highly BOARD F EFFECT OF MENTHOL ON POST-EXERCISE MUSCLE conserved protein composed of three domains, the A- and B-domain, and an SORENESS. RYAN T. TERRY. 455 WOODLAWN AVE., SPRINGFIELD OH 45504. acidic tail at it's C-terminus. HMG-1 has been implicated in many processes Counterirritation involves the masking of one pain with the induction such as replication, transcription, chromatin assembly and development. The of another pain. Chemical counterirritants are used widely for the treatment of A-and B-domains are canonical HMG boxes and are isostructural, but do not sore muscles, but they have been studied insufficiently. Menthol, a common contain identical sequences. The B-domain of HMG-1 contains a sequence, ingredient in nonprescription chemical counterirritants, has qualities that may LXCXE, that has been shown to be crucial for binding to the Retinoblastoma be able to ease the pain of sore muscles when applied topically. Subjects protein, pRb. This sequence is present in a few viral oncoproteins, as well as whowere unaccustomed to upper body workouts engaged in a regimen of other cellular proteins that bind to the pocket region of pRb. pRb exerts its effect eccentric exercise on the elbow flexors. After 48 hours, when soreness during the cell cycle in G1 phase. Briefly, in early G1 phase, pRb is complexed generally reaches its peak, the subjects returned to the laboratory, where with a transcription factor, E2F, as the cell progresses, pRb becomes phospho- menthol or a placebo were tested for effects on soreness ratings and EMG rylated and releases E2F which allows the cell to enter S phase. Alternatively, activity. Menthol was ineffective in alleviating this soreness, and it did not affect certain viral oncoproteins bind to pRb and release E2F, this then results in the EMG measurements. Using the theory of metaesthesia, menthol seems to uncontrolled cell proliferation. We have used a GST-capture experiment with stimulate nociceptors at a low level and induces a burning feeling that may or a number of truncated GST-Rb fusion proteins to explore the interaction may not be perceived by subjects as painful.
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