Knowledge and attitudes toward sexuality in adolescents and their association with the family and other factors

Family structure and function and their association with knowledge and attitudes toward sexuality, contraception, and sexually transmitted diseases (STD) were studied in 918 students and 312 adolescents working in factories. Unmarried workers reported higher rates of sexual activity than did students (30.9% vs. 21.8%, p = .04 for males; 12.9% vs. 6.0%, p = .005 for females). Among sexually active males, 33.3% of students and 30.7% of workers used contraception, compared with 27.5% of female students and 9.5% of female workers. Workers were from larger families than students, and the male and female workers had lower scores for knowledge on sexuality, contraception, and STD than did students. Multiple stepwise regression showed that age and schooling of the parents were associated with knowledge and attitudes in the students. In workers, the position of the child in the family was a negative regressor for attitudes and knowledge on sexuality in males, and for knowledge on contraception and STD in females. In regard to family function, the significant factors were compromise between the parents, positive affective response, communication within the family, problem solution, and control of behavior. It was concluded that female workers are at higher risk for unwanted pregnancies and STD. The factors associated with knowledge and attitudes were age, schooling of the parents, mother working out of home, position of the adolescent in the family, and the diverse aspects of family function.     

Pathogenesis of Mycobacterium bovis infection in cattle

This paper reviews the pathogenesis of Mycobacterium bovis infection in cattle, focusing on aspects relating to the host rather than the organism. A broad concept of pathogenesis has been considered and information is presented on sources and routes of infection, as well as the immune responses and pathology. In addition, data is presented on the excretion of M. bovis from tuberculous cattle.     

Multiple solution conformations of the integrin-binding cyclic pentapeptide cyclo(-Ser-D-Leu-Asp-Val-Pro-). Analysis of the (phi, psi) space available to cyclic pentapeptides

The aqueous solution structure of the cyclic pentapeptide cyclo(-Ser-D-Leu-Asp-Val-Pro-) has been determined by two-dimensional 1H-NMR spectroscopy, combined with a conformational search and distance-geometry calculations. As many as five conformers in slow exchange were observed, and the rate of interconversion between components was measured from the build-up rates of exchange peaks. NMR data allowed the structures of the two predominant conformers to be determined. The major component (66%) contained a cis-proline as part of a type-VIa2 beta-turn encompassing residues Asp-Val-cis-Pro-Ser. The second component (16%) contained only trans-amide bonds, and a type-VIII beta-turn formed by residues Val-Pro-Ser-D-Leu. These structures are discussed in relation to the (phi, psi), space available to the cyclic pentapeptide, determined by a conformational search, and in relation to previously published cyclic-pentapeptide structures. The molecule exhibits activity in a scintillation-proximity assay for the inhibition of the interaction between the integrin very-late antigen-4 (VLA-4; alpha 4 beta 1) and vascular-cell-adhesion molecule-1 (VCAM-1). The structure/activity relationship of the LDV sequence is discussed and related to the recently published X-ray structure of VCAM-1. The relevance of the work to the design of anti-inflammatory drugs is discussed.     

Purification and characterization of a NADP+/NADPH-specific flavoprotein that is overexpressed in FdI- strains of Azotobacter vinelandii

Earlier studies have established that mutant strains of Azotobacter vinelandii that do not synthesize ferredoxin I (AvFdI) overexpress another protein designated Protein X (Morgan, T. V., Lundell, P. J., and Burgess, B. K. (1988) J. Biol. Chem. 263, 1370-1375). This protein has now been purified using two-dimensional gel electrophoresis as an assay. The purified protein is a monomer with M(r) approximately 29,000 which degrades slowly to a specific M(r) approximately 22,000 form when stored in solution. The native protein is bright yellow and contains noncovalently attached FAD that is reduced by either dithionite or NADPH without formation of a stable semiquinone. Titration with NADP+/NADPH gives an E0' value of approximately -327 mV versus SHE. Because this E0' is so close to that of the NADP+/NADPH couple it is not clear if Protein X is an NADPH oxidase or an NADP+ reductase in vivo. Comparison of the NH2-terminal sequence and other properties of Protein X with those of other proteins, suggests that it is likely to be related to the Escherichia coli ferredoxin NADP+ reductase (the fpr gene product), and affinity chromatography shows that Protein X binds specifically to AvFdI.