Rabbit brain

FIGURE 6 Distribution of [ HlBCNU-associated radioactivity time in rabbit brain. The distribution of radioactivity was measured using quantitative autoradiography techniques following implantation of discs described for Fig. 5 into the brains of rabbits. Details of the experimental procedure are described in the text. 

Brem, H., Kader, A., Epstein, J. I., Tamargo, R., Domb, A., Danger, R., and Leong, K., Biocompatibility of bioerodible controlled release polymers in the rabbit brain. Selective Caacer Therapeutics. 5, 55-65, 1989. 

Pharmacological Methods and Results. The data upon which the following discussion is based were accumulated using three techniques mouse bioassay, displacement of radiolabelled saxitoxin from rabbit brain membranes, and blockage of sodium conductance through rat sarcolemmal sodium channels incorporated into planar lipid bilayers. The results are summarized in Figures 11 and 12. 

Binding assays for the saxitoxins were conducted with homogenized rabbit brain and saxitoxin exchange-labelled with tritium at C-11 (92, 93). If the various saxitoxins were available with suitably intense radiolabels, then the equilibrium dissociation constant, K, could be measured directly for each. Since only saxitoxin is currently available with the necessary label, the binding experiments instead measure the ability of a compound to compete with radiolabelled saxitoxin for the binding site. The value obtained, Kj, corresponds to the uilibrium dissociation constant, K, that would be observed for the compound if it were measured directly. Affinity is defined for this assay as the reciprocal of Kj. The affinities of several of the saxitoxins (94) are summarized in Figure 11, expressed relative to saxitoxin and plotted on a logarithmic scale. 

Braun, C. M. Pivik, R. T. (1981). Effects of locus coeruleus lesions upon sleeping and waking in the rabbit. Brain Res. 230, 133-51. 

Longo, V. G. Silvestrini, B. (1957). Action of eserine and amphetamine on the electrical activity of the rabbit brain. J. Pharmacol. Exp. Ther. 120, 160-70. 

Neumann, P.E. and F. Taketa. 1987. Effects of triethyltin bromide on protein phosphorylation in subcellular fractions from rat and rabbit brain. Mol. Brain Res. 2 83-87. 

Du W, Aloyo VJ, Harvey JA. (1997). Harmaline competitively inhibits [3H]MK-801 binding to the NMDA receptor in rabbit brain. Brain Res. 770(1-2) 26-29. 

P.N. Venkatasubramanian, Y.J. Shen, A.M. Wyrwicz, In vivo F one-dimensional chemical shift imaging study of isoflurane uptake in rabbit brain, NMR Biomed. 6 (1993) 377-382. 

Suda, Isamu and A. C. Kito, Histological Cryoprotection of Rat and Rabbit Brains, Cryoletters 5 33, 1966. 

M. Samira et al. G115 extract increases the glucose uptake and utilization in rabbits brain... 

Creatine kinase sequences are known for many different species and iso-forms, so species-specificity of MAbs can often be used for refining the details of epitope mapping. Natural variants that prevent MAb binding are likely to involve contact residues, because the overall protein structures (and enzyme activity) are likely to be retained. The CK-2A7 MAb in Fig. IB binds between Met-29 and Cys-73. It recognizes rabbit and Torpedo CKs, as well as chick CK, but it fails to bind to either rat muscle CK or rabbit brain CK. This suggests that Lys-39 is required for CK-2A7 binding, since it is replaced by Asn m rat muscle CK and by Ala in rabbit brain CK (7), and is the only amino acid change consistent with the observed CK-2A7 specificity. 

AMP aminohydrolase, an enzyme relatively specific for AMP, has been observed in reptiles (44), erythrocytes (38), snail (45), unfertilized fish eggs (46), invertebrates (47), a variety of mammalian tissues (20), and a particulate fraction of pea seeds (48). Evidence suggests that the frog muscle AMP aminohydrolase is located within or just beneath the sarcolemma (49). The rabbit skeletal and heart muscle enzymes were found in the cytoplasm and mitochondria (20, Jfi, 50, 51), while the enzyme of kidneys and gills of freshwater fish was located in the cytoplasmic fraction (52). The enzyme occurs in most areas of the rat (53) and rabbit brain (54). The nonspecific enzyme from several microbial sources deaminates adenosine triphosphate (ATP) and adenosine diphosphate (ADP) as well as AMP (see Section V). 

Some investigators have found the enzyme primarily in the 100,000 X g supernatant fluid of extracts of rabbit brain (37), dog heart (42), rat liver (45), rat brain, and beef pineal gland (48). In contrast, other investigators have reported that the enzyme from beef heart (36) and rat brain (49, 50) is mostly particulate being present in all the primary fractions nuclear, mitochondrial, microsomal, and 100,000 X 9 supernatant. The reasons for these discrepancies are not entirely clear but most likely result from differences in fractionation technique. Evidence from density gradient procedures coupled with electron microscopic examination indicate that the enzyme is preferentially located at nerve... 

Chlorpromazine and other phenothiazines Rabbit brain — Significant at 0.05 (64)... 

Limberger N, Spath L, Starke K (1988) Presynaptic a2-adrenoceptor, opioid k-receptor and adenosine Aj-receptor interactions on noradrenaline release in rabbit brain cortex. Naunyn-Schmiedeberg s Arch Pharmacol 338 53-61. 

Obal F Jr, Opp M, Cady AB, Johannsen L, Krueger JM. Prolactin, vasoactive intestinal peptide, and peptide histidine methionine elicit selective increases in REM sleep in rabbits. Brain Res 1989 490 292-300. 

V.M. Tennyson, M. Budlninkas-Schoenebeck and P. Gershon, Effects of chronic reserpine treatment on development of maturity of the putamen in fetal rabbits, Brain Res. Bull., 9(1-6) (1982) 651-662. 

Lim WK, Myung C-S, Garrison JC et al (2001) Receptor-G protein y specificity yll shows unique potency for Ai adenosine and 5-HTia receptors. Biochemistry 40 10532-41 Limberger N, Spath L, Starke K (1988) Presynaptic a2-adrenoceptor, opioid K-receptor and adenosine Al-receptor interactions on noradrenaline release in rabbit brain cortex. Naunyn-Schmiedberg s Arch Pharmacol 338 53-61... 

Waeber C, Palacios JM. Non 5-HT1A/5-HTlc [3H]5-HT binding sites in the hamster, opossum and rabbit brain show similar regional distribution but different sensitivity to beta-adrenoceptor antagonists. Synapse 1992 12 261-270. 

Guimbal, C. Kilimann, M.W. (1993). A Na+-dependent creatine transport in rabbit brain, muscle, heart and kidney. cDNA cloning and functional expression. J. Biol. Chem. 268, 8418-8421. 

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