The Brown Modification of the Thouless Test of Religious Orthodoxy and three personality measures were administered to 82 students in introductory psychology. The Manifest Anxiety Scale, Manifest Hostility Scale, and a variation of the Coopersmith Self-esteem Inventory were utilized to determine a profile for individuals with orthodox religious beliefs. The correlation between the Thouless test and the Manifest Hostility Scale was significant in that highly orthodox individuals scored lower than other subjects on the Manifest Hostility Scale. There were significant but small correlations among the personality variables but no other trends were noted in relation to religious orthodoxy.
The Allport-Vernon-Lindzey Study of Values and the Brown Modification of the Thouless Test of Religious Orthodoxy were administered to 120 male and female students in introductory psychology. Measures of anxiety, self-esteem, authoritarianism, and humanitarianism were also administered to the Ss in an effort to determine whether the two measures of religiosity would yield different personality and attitude profiles of the "religious" individual. A significant positive correlation was found between authoritarianism and the Thouless Test and between humanitarianism and the Study of Values religious measure. All other correlations involving the two measures of religiosity were found to be nonsignificant. These findings lend support to the notion that using two divergent measures of religiosity does result in the formation of different profiles of the "religious" individual.
To attempt to locate functionally important regions of the interferon (IFN) molecule, recombinant human IFN-a2 was subjected to proteolytic digestion. The bacterial proteinase thermolysin produced two major complementary fragments, and . After reduction with 2-mercaptoethanol and separation of the two major fragments on NaDodSO4/polyacrylamide gel electrophoresis, antiviral activity persisted in the larger, Mr 12,000, fragment consisting of the amino-terminal 110 amino acids.The availability of large amounts of recombinant DNA-derived interferon (IFN) has fostered investigation of IFN's structure-function relationships; however, the specific structural features required for biologic activity remain largely unknown. Despite disul'ide bond assignment (1), secondary structure measurements (2), and investigation of novel recombinant IFNs, (3, 4), little information is available as to which areas of the protein may be functionally important. Modification of the structure of IFNs by using a variety of enzymes and chemicals has yielded varied results. Incubation of IFNs with glycosidic enzymes in general does not appear to alter the antiviral activity (5). Cleavage of IFNs with endopeptidases such as trypsin or with chemicals such as cyanogen bromide has thus far been unsuccessful in generating active fragments (6, 7). In contrast, some active species were obtained after treatment with exopeptidases (8), pepsin (9), and periodate (10); however, reductions in size were modest with the active species of Mr 15,000 or larger. To attempt to identify small functional portions of the IFN molecule we have studied proteolytic fragments of a recombinant human IFN, HuIFN-a2, produced by the bacterial proteinase thermolysin. We report here that proteolysis of this IFN with thermolysin generates a biologically active fragment originating from the amino-terminal end of the molecule. MATERIALS AND METHODSThermolysin was obtained from Calbiochem. HuIFN-a2 (1.5x 10' units/mg of protein) was the gift of Schering. HuIFNaA (2.0 x 108 units/mg of protein) was the gift of HoffmannLa Roche. 125I-labeled HuIFN-aA (1251-HuIFN-aA) was prepared as described (11).Preparative NaDodSO4/polyacrylamide gel electrophoresis (NaDodSO4/PAGE) was performed according to the method of Laemmli (12). The separating gels were 16% acrylamide/N,N'-methylene bisacrylamide, 0.75 mm in thickness and 12 cm in length. Electrophoresis was performed at 15 mA per slab gel. The gels were stained and destained as described (13). The stained gel bands were sliced from the gel and eluted as reported (13). The samples were then assayed for biological activity or dialyzed and lyophilized for amino acid analysis and amino acid sequence determination as described (14). Continuous elution of IFN fragments was done by the method of Hunkapiller (unpublished data).IFN antiviral assays were performed by using Madin-Darby bovine kidney (MDBK) cells or human foreskin fibroblasts with vesicular stomatitis virus as reported (15). Competitive receptor binding assays using 125I-H...
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