Concentration of monoamines in the brain of minks differing in their reaction to man

Content of dopamine in the striatum; of serotonin, 5-hydroxyindolacetic acid and noradrenaline in the hypothalamus, striatum and midbrain was studied in three groups of minks from population of an animal farm, differing by their reaction to humans (cowardly, calm, aggressive). The reaction to humans was estimated by a system of marks at the attempt to catch the mink with a mitten. Aggressive animals had a lowered level of serotonin in the hypothalamus and striatum, a lesser content of serotonin metabolite--5-hydroxyindolacetic acid in the striatum. Minks of different groups did not differ by noradrenaline content, but dopamine level in the striatum of cowardly minks was higher than in calm and aggressive animals. Conclusion is made that polymorphism of behaviour corresponds to polymorphism of the state of monoaminergic systems.     

Changes in the amino acid sequence of hemagglutinin during sequential adaptation of human influenza virus A to replication in mice

The primary structure of hemagglutinin (HA) gene of Influenza virus A/USSR/90/77 (H1N1) variants after 3 and 11 passages has been determined. In the HA1 coding region of mice-adapted virus (11 passages) there are two amino acid substitutions: Thr 89----Ala and Asn 127----Asp. At the first stage of adaptation (3-rd passage) only a single mutation was detected: Asn 127----Asp. The adaptation is accompanied by the loss of specific carbohydrate attachment sites adjacent to the receptor-binding site located at HA1 subunit with a concomitant variation in antigenicity.     

Determination of the relative and absolute stereochemistry of a potent and α1A-selective adrenoceptor antagonist

The binding affinities and selectivities of antagonists Figure 1 and Scheme 2 for the α_1A-adrenoceptor are dependent on the stereochemical orientation of the groups at the C-4 and C-5 positions of the oxazolidinone ring. The unambiguous assignment of the relative and absolute configurations of the diastereomers of SNAP 7915 (Figure 1 and Scheme 2) is reported.     

Gastrointestinal microflora,food components and colon cancer prevention

Evidence that the intestinal microbiota is intrinsically linked with overall health, including cancer risk, is emerging. Moreover, its composition is not fixed but can be influenced by several dietary components. Dietary modifiers, including the consumption of live bacteria (probiotics) and indigestible or limited digestible food constituents such as oligosaccharides (prebiotics) and polyphenols or both (synbiotics), are recognized modifiers of the numbers and types of microbes and have been reported to reduce colon cancer risk experimentally. Microorganisms also have the ability to generate bioactive compounds from food components. Examples include equol from isoflavones, enterodiol and enterolactone from lignans and urolithins from ellagic acid, which have also been demonstrated to retard experimentally induced cancers. The gastrointestinal microbiota can also influence both sides of the energy balance equation, namely, as a factor influencing energy utilization from the diet and as a factor that influences host genes that regulate energy expenditure and storage. Because of the link between obesity and cancer incidence and mortality, this complex complexion deserves greater attention. Overall, a dynamic interrelationship exists between the intestinal microbiota and colon cancer risk, which can be modified by dietary components and eating behaviors.     

Monoclonal antibodies to alpha-chain regions of human fibrinogen that participate in polymer formation

Monoclonal antibodies have been generated against a cross-link-containing derivative of alpha polymer (alpha XLCNBr), isolated following CNBr digestion of fibrin [Sobel, J. H., Ehrlich, P. H., Birken, S., Saffran, A. J., & Canfield, R. E. (1983) Biochemistry (preceding paper in this issue)]. One cloned cell line (F-102) was chosen for characterization based on its apparent specificity for the A alpha-chain region A alpha 518-584 (CNBr X). A second line (F-103) was selected because of its anti-A alpha 241-476 (CNBr VIII) properties. These two regions of the A alpha chain have previously been implicated as major contributors to the cross-linking process that leads to alpha-polymer formation. Radioimmunoassays have been developed, employing the immunoglobulins produced by clones F-102 and F-103. These assays have been applied, in conjunction with high-performance liquid chromatography purified tryptic and chymotryptic derivatives of CNBr VIII and CNBr X, to localize the respective determinants involved in antibody binding. In each case, virtually full immunoreactivity was exhibited by both the CNBr fragment and a single tryptic or chymotryptic peptide originating from it. These findings indicate that sequence-specific, rather than conformational, determinants were operative in the generation of antibodies F-102 and F-103. The epitope recognized by F-102 was localized to the region of A alpha 540-554, while the F-103 binding site resided within A alpha 259-276. When these radioimmunoassays were applied to study the relative immunoreactivity exhibited by a variety of fibrinogen derivatives, the results obtained support earlier suggestions that the COOH-terminal portion of the A alpha chain contains regions of random conformation.