A comparative study of memory for olfactory discriminations: Dogs (Canis familiaris), rats (Rattus norvegicus), and humans (Homo sapiens).

2020 ◽  
Vol 134 (2) ◽  
pp. 170-179 ◽  
Author(s):  
Gordon Ka-Ho Lo ◽  
Krista Macpherson ◽  
Hayden MacDonald ◽  
William A. Roberts
Keyword(s):  
Comparative Study ◽  
Rattus Norvegicus ◽  
Homo Sapiens ◽  
Canis Familiaris

scholarly journals In Silico Investigation of Luminol, Its Analogues and Mechanism of Chemiluminescence for Blood Identification Beyond Forensics

2020 ◽  
Vol 14 (2) ◽  
pp. 117-127
Author(s):  
Toluwase H. Fatoki
Keyword(s):  
Rattus Norvegicus ◽  
In Silico ◽  
Homo Sapiens ◽  
Canis Familiaris ◽  
Amino Acid Residues ◽  
Molecular Binding ◽  
Binding Score ◽  
In Silico Study ◽  
Fluorescent Products ◽  
New Methodologies

Objective: This study aimed at discovering chemiluminescent analogues of luminol, predict their molecular binding to hemoglobin of bloodstains in household crime, and expound the mechanism of chemiluminescence of luminol. Materials and Methods: Similarity and clustering analyses of luminol analogues were conducted, and molecular docking was carried out using hemoglobin from Homo sapiens and four domestic organisms namely Gallus gallus, Drosophila melanogaster, Rattus norvegicus, and Canis familiaris. Results: The results showed the order of overall binding score as D. melanogaster > H. sapiens > C. familiaris > R. norvegicus > G. gallus. Seven compounds namely ZINC16958228, ZINC17023010, ZINC19915427, ZINC34928954, ZINC19915369, ZINC19915444, and ZINC82294978, were found to be consistently stable in binding with diverse hemoglobin and possibly have chemiluminescence than luminol in this in silico study. The interaction of human hemoglobin with luminol and its analogues, showed that amino acid residues His45, Lys61, Asn68, Val73, Met76, Pro77, Ala79, Ala82, Leu83, Pro95, Phe98, Lys99, Ser102, Ser133, Ala134, and Thr134, were possibly significant in the mechanism of action of presumptive test compounds. It was hypothesized that the improved mechanism of chemiluminescent for the identification of blood was based on peroxidase-like reaction, that produces nitric oxide which binds to hemoglobin (Hb) and inhibits Hb degradation without yielding fluorescent products. The compound 2,3-benzodioxine-1,4,5(6H)-trione was formed, which possibly emits light. Conclusion: This study provides novel insight on the luminol and its expanded mechanism for broader possible applications with careful development of new methodologies.

scholarly journals In-Silico Investigation of Luminol, Its Analogues and Improved Mechanism of Chemiluminescence for Blood Identification Beyond Forensics

2020 ◽  
Author(s):  
Toluwase Hezekiah Fatoki
Keyword(s):  
Rattus Norvegicus ◽  
Homo Sapiens ◽  
Canis Familiaris ◽  
Amino Acid Residues ◽  
Molecular Binding ◽  
Binding Score ◽  
Actual Mechanism ◽  
Nitrosonium Cation ◽  
Fluorescent Products ◽  
New Methodologies

ABSTRACTThis study aimed to discover chemiluminescent analogues of luminol, understand their molecular binding to hemoglobin of bloodstains in the household crime, and the mechanism of chemiluminescence. Similarity and clustering analyses of luminol analogues were conducted, and molecular docking was carried out on hemoglobin from Homo sapiens and other four domestic organism namely Gallus gallus, Drosophila melanogaster, Rattus norvegicus, and Canis familiaris. The results show that the order of overall binding score is D. melanogaster > H. sapiens > C. familiaris > R. norvegicus > G. gallus. Seven compounds namely ZINC16958228, ZINC17023010, ZINC19915427, ZINC34928954, ZINC19915369, ZINC19915444, and ZINC82294978, were found to be consistently stable in binding to diverse hemoglobin and possibly have chemiluminescence than luminol. The amino acid residues involved in the interaction of human hemoglobin with the 30 test compounds, show that His45, Lys61, Asn68, Val73, Met76, Pro77, Ala79, Ala82, Leu83, Pro95, Phe98, Lys99, Ser102, Ser133, Ala134, and Thr134 are significant in the mechanism of action of presumptive test compounds. The improved mechanism of chemiluminescent identification of blood hypothesized that nitrite interact with the Fe(II) heme, with the cleavage of a hydroxide ion and the formation of the nitrosonium cation in peroxidase reaction. It was proposed that degradation of rhombic heme complex to fluorescent products is possibly inhibited by nitric oxide from the test compound luminol. This study provides novel insight on the luminol and its actual mechanism for broader possible applications of luminol with careful development of new methodologies.

scholarly journals The easy-to-hard effect in human (Homo sapiens) and rat (Rattus norvegicus) auditory identification.

2008 ◽  
Vol 122 (2) ◽  
pp. 132-145 ◽  
Author(s):  
Estella H. Liu ◽  
Eduardo Mercado ◽  
Barbara A. Church ◽  
Itzel Orduña
Keyword(s):  
Rattus Norvegicus ◽  
Homo Sapiens

Factors determining the distribution of introduced mammals in nature reserves of the southern province, New Caledonia

2003 ◽  
Vol 30 (2) ◽  
pp. 187 ◽  
Author(s):  
Sophie Rouys ◽  
Jörn Theuerkauf
Keyword(s):  
Rattus Norvegicus ◽  
New Caledonia ◽  
Canis Familiaris ◽  
Rattus Rattus ◽  
Nature Reserves ◽  
House Mice ◽  
Mus Musculus Domesticus ◽  
Southern Province ◽  
Feral Populations ◽  
Norway Rats

We studied the distribution of introduced mammals in six nature reserves of New Caledonia's southern province. Polynesian rats (Rattus exulans) were common in both rainforest and shrubland but their abundance decreased with increasing altitude. Ship rats (Rattus rattus) were abundant in rainforest but less numerous in shrubland and their abundance did not increase with altitude. We found no Norway rats (Rattus norvegicus) or house mice (Mus musculus domesticus) in reserves. Feral pigs (Sus scrofa) used mainly rainforest but also shrubland and preferred foraging in valleys with alluvial soils. Rusa deer (Cervus timorensis) selected shrubland over rainforest. Feral cats (Felis catus) were widely distributed in the reserves, whereas dogs (Canis familiaris) strayed into reserves but did not form feral populations.

scholarly journals Thermophilic, Reversible γ-Resorcylate Decarboxylase from Rhizobium sp. Strain MTP-10005: Purification, Molecular Characterization, and Expression

2004 ◽  
Vol 186 (20) ◽  
pp. 6855-6863 ◽  
Author(s):  
Masahiro Yoshida ◽  
Nobuhiro Fukuhara ◽  
Tadao Oikawa
Keyword(s):  
Rattus Norvegicus ◽  
Homo Sapiens ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Hypothetical Protein ◽  
Cell Extract ◽  
Amino Acid Residues ◽  
Sequence Identities ◽  
Rhizobium Sp

ABSTRACT We found the occurrence of thermophilic reversible γ-resorcylate decarboxylase (γ-RDC) in the cell extract of a bacterium isolated from natural water, Rhizobium sp. strain MTP-10005, and purified the enzyme to homogeneity. The molecular mass of the enzyme was determined to be about 151 kDa by gel filtration, and that of the subunit was 37.5 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; in other words, the enzyme was a homotetramer. The enzyme was induced specifically by the addition of γ-resorcylate to the medium. The enzyme required no coenzyme and did not act on 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 2-hydroxybenzoate, or 3-hydroxybenzoate. It was relatively thermostable to heat treatment, and its half-life at 50°C was estimated to be 122 min; furthermore, it catalyzed the reverse carboxylation of resorcinol. The values of k cat/Km (mΜ−1 · s−1) for γ-resorcylate and resorcinol at 30°C and pH 7 were 13.4 and 0.098, respectively. The enzyme contains 327 amino acid residues, and sequence identities were found with those of hypothetical protein AGR C 4595p from Agrobacterium tumefaciens strain C58 (96% identity), 5-carboxyvanillate decarboxylase from Sphingomonas paucimobilis (32%), and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylases from Bacillus cereus ATCC 10987 (26%), Rattus norvegicus (26%), and Homo sapiens (25%). The genes (graA [1,230 bp], graB [888 bp], and graC [1,056 bp]) that are homologous to those in the resorcinol pathway also exist upstream and downstream of the γ-RDC gene. Judging from these results, the resorcinol pathway also exists in Rhizobium sp. strain MTP-10005, and γ-RDC probably catalyzes a reaction just before the hydroxylase in it does.

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