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Sectional Meetings SECTIONAL MEETINGS Details of technical meetings follow. See map for building locations. Business meetings are scheduled for each section. An important item of business is the election of officers. I f o ZOOLOGY A. ZOOLOGY MORNING SESSION, SATURDAY APRIL 24, 1982 DENNEY HALL ROOM 207 DAVID H. STANSBERRY, PRESIDING MITOCHONDRIAL MALATE UTILIZATION AND NADPH-NAD TRANSHYDROGENATION IN ADULT HYMENOLEPIS DIMINUTA (CESTODA). Jeffrey R. McKelvey and Carmen F. Fioravanti. Department of Biological Sciences, Bowling Green State University, Bowling Green, Ohio 43403. Physiologically, Hymenolepis diminuta is energetically anaerobic. Cytosolic malate, arising from glucose catabolism, serves as the substrate for a mitochondrial dis- mutation reaction, leading to anaerobic ATP generation. Presumably, mitochondrial, NADP-speci- fie, "malic" enzyme is the source of required reducing equivalents. However, electron trans- port in H. diminuta requires NADH. Thus, a mechanism is necessitated for hydride ion transfer from NADPH to NAD, if "malic" enzyme is the source of reducing power. The H. diminuta, mito- chondrial NADPH:NAD transhydrogenase would fulfill a hydride-transfer function. In this study, the cestode's transhydrogenase was found to be unaffected by Mn++ion, and the specificity of "malic" enzyme for NADP and Mn++ion was confirmed. Significantly, coupling of "malic" enzyme with transhydrogenation was demonstrated, since Mn++ion stimulated acetylpyridine NAD reduction when malate and NADP were present in the assay system. The tandem catalytic activity of NAD- linked, malate dehydrogenase and oxalacetate decarboxylase did not account for the required NADH accumulation. These data are consistent with the supposition that indeed the "malic" enzyme and transhydrogenase are required for anaerobic phosphorylation. Supported by NIH 5- R01-AI-15597 and 1-K04-AI-00389. USPHS. ENZYMATIC ACTIVITIES ASSOCIATED WITH THE MICROSOMAL FRACTION OF ADULT HYMENOLEPIS DIMINUTA (CESTODA). Curtis L. Batten and Carmen F. Fioravanti, Department of Biological Sciences, Bowling Green State University, Bowling Green, Ohio 43403 Energetically, the adult intestinal cestode, Hymenolepis diminuta, is essentially anaerobic and succinate accumulates as the major end-product of glucose dissimila- tion. Physiologically, mitochondrial ATP generation occurs via an electron transport-associated, fumarate reductase system without the need for oxygen. However, despite this anaerobic nature, H. diminuta assimilates oxygen when available indicating that oxygen may be involved in meta- bolic processes other than energy generation. Studies with the microsomal fraction of H. dimi- nuta suggest that, in part, oxygen utilization may be the result of enzymatic components associated with this fraction. Based on the distribution of succinate dehydrogenase activity, prepared H. diminuta microsomes appear to be relatively free of mitochondrial contamination Oxygen utilization by the microsomes is apparent in that this fraction catalyzes a reduced pyridine nucleotide oxidase activity (NADH or NADPH). This NAD(P)H oxidase has been found to be insensitive to both rotenone and antimycin A. Moreover, an NAD(P)H-coupled cytochrome c reductase is displayed with NADH being the preferred reductant. Whether this cytochrome c reductase activity is an indicator of cytochrome P-450 involvement (and therefore mixed-function oxygenation remains to be determined. Interestingly, H. diminuta microsomes also exhibit an NADPH:NAD transhydrogenation mechanism as assessed by acetylpyridine NAD reduction Supported by NIH 5-R01-AI-15597 and 1-K04-AI-00389, USPHS. APPARENT SUBSTRATE-INDUCED CONFORMATIONAL CHANGE OF ADULT HYMENOLEPIS DIMINUTA (CESTODA), MITOCHONDRIAL NADPH:NAD TRANSHYDROGENASE. Denise A. Malcuit and Carmen F. Fioravanti. Department of Biological Sciences, Bowling Green State University, Bowling Green, Ohio 43403 The mitochondrial NADPH:NAD transhydrogenase of H. diminuta, catalyzes a hydride ion transfer from NADPH to NAD, producing NADH. As such, this enzyme serves a vital function in the anaerobic energetics of the cestode by linking the mitochondrial, NADP-specific "malic" enzyme with the NADH-requiring, electron transport-associated, fumarate reductase system. Recent studies, dealing with thermal denaturation, revealed that the H. diminuta, NADPH:NAD transhydrogenase is subject to substrate-dependent conformational variation. Transhydrogenase activity was assessed by the reduction of acetylpyridine NAD employing isolated mitochondrial membranes as the enzyme-source. The rate of thermal inactivation of the transhydrogenase was accelerated markedly by the addition of NADPH or NADP to the system. NADPH was the more effective in increasing thermal lability. The increased thermal lability was dependent upon substrate concentration. Whether NADH or NAD alters the enzyme's thermal inactivation profile remains to be determined. However, the data obtained indicate that the transhydrogenase undergoes substrate-induced conformational change which, in turn, would be consistent with the supposition that proton translocation may be associated with this transhydrogenation. Supported by a Sigma-X1 Grant-in-Aid-of-Research and NIH 1-K04-AI-00389, USPHS. ZOOLOGY THE SPECIFIC DISTINCTNESS OF TOXOLASMA LIVIDUS (RAFINESQUE, 1831) AND TOXOLASMA CYLINDRELLUS (LEA, 1868) (MOLLUSCA:BIVALVIA:UNIONOIDA). David H. Stansbery, Ohio 9.15 State University Museum of Zoology, 1813 N. High St., Columbus, OH 43210. Taxa in the unionid genus Toxolasma Rafinesque, 1831 have been plagued with system- atic and nomenclatural problems since their description (Barnes 1823, Rafinesque 1831, Lea 1831-1869, and Conrad 1838) over a century ago. Toxolasma lividus and T_. cylindrellus were originally described as distinct taxa but, due to their superficial similarity, they were soon relegated either to subspecies status or synonymized. A recent study of 128 lots compris- ing 536 specimens of _T. lividus and 74 of T. cylindrellus reveals these names to represent two distinct taxa. These species differ in growth rate, maximum size, proportions, degree of sexual dimorphism in the shell, color of periostracum and color of the nacre. HOST-COMMENSAL RELATIONSHIPS OF CRAYFISHES AND OSTRACODS OF THE GULF COASTAL PLAIN, U.S.A. H. H. Hobbs III, Department of Biology, P. 0. Box 720, Wittenberg University, 9:30 Springfield, Ohio. 45501. Crayfishes from the south-central Gulf Coastal Plain were individually collected from streams, roadside ditches, and burrows and were examined for epizootic ento- cytherid ostracods. Thirty-four species of ostracods, representing nine genera were encountered, of which 15 were undescribed species: Ankylocythere (15), Daetylocythere (1), Entocythere (4), Geocythere (3), Hartocythere (1), Ornithocythere (3), Saurocythere (1), Ther- mastrocythere (1), and Uncinocythere (5). Twenty-one species (61.8%), five genera, were ubiqui- tous, being found on burrowing crayfishes inhabiting seepage areas, flatwoods, and floodplains of streams and also were collected from crayfishes found in ditches, ponds, lakes and streams. Ankylocythere sinuosa (Rioja) had the largest geographical range and was found on the greatest number of hosts of any of the ostracods on the plain. Eight species (23.5%), three genera, demonstrated "ecological specificity" as they were associated with multiple crayfish hosts which spend all or most of their lives in burrows. Five species (14.7%), four genera, of ostra- cods were restricted to a single primary burrowing crayfish host, Cambarus (Lacunicambarus) diogenes diogenes Girard; Geocythere geophila (Hart), Hartocythere torreya (Hart), Ornithocy- there aetodes Hobbs, Ornithocythere gypodes Hobbs, and Saurocythere rhipis Hobbs. Other ostra- cod species were found in the same localities on different hosts and some of these same ostra- cods were found also on C. (L_.) d. diogenes; this adds credence to an assumption of host speci- ficity for these five species. RHTHMIC SECRETION FROM THE HEPATOPANCREAS OF THE CRAYFISH, ORCONECTES RUSTICUS, AND A SECRETORY RESPONSE TO CAERULEIN. Natalie Schoch and 9:45 E. J. DeVillez, Dept. of Zoology, Miami University, Oxford, Ohio 45056 Gastric juice samples and hepatopancreatic extracts were obtained from a population of previously starved O. rusticus at half hour intervals following a brief period of feeding. Tryptic activity in the gastric juice displayed a cycling pattern with maxima at 0.5 and 3.5 to 4.0 hours after feeding. Tryptic activity in hepatopancreatic extracts fluctuated greatly showing maxima at the onset of feeding and at 1.0 and 5.5 hours after feeding. Biological activity of the hormone, caerulein, was also examined. Doses of 5 ug/0.1 ml caerulein were given to a group of starved crayfish. Sham injections containing cytochrome c were administered to a second starved population. In each case, gastric juice samples were obtained at 1.0 and 4.0 hours after injection. Tryptic activities in the gastric juice samples from the caerulein injected animals at 4.0 hours after injection were significantly higher than the activities of the cytochrome c injected animals at either time. No significant changes were observed in amylase activities. THE PHYLOGENY OF THE SUBGENUS CAMBARUS AND THE CAMBARUS BARTONII BARTONII COMPLEX (DECAPODA: CAMBARTDAE). Roger F. Thema, The Ohio State University Museum, Ohio State University,Columbus, Ohio 1+3210. Multivariate analysis was performed on 830 specimens of the subgenus Cambarus, formerly considered to be 4 species. My analysis
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