Evaluation of the Hybrid Capture 2 CT/GC DNA tests and the GenProbe PACE 2 tests from the same male urethral swab specimens.

Background: A previous study demonstrated that Digene's Hybrid Capture 2 (HC2) DNA tests for detection of and (CT/GC) could be performed using cervical swab specimens collected in GenProbe transport media with significantly greater sensitivity for the detection of than with the GenProbe PACE 2 system.

Goal: The goal was to assess the performance of HC2 tests in comparison with GenProbe PACE 2 tests for the detection of CT/GC in male urethral swab specimens.

Study Design: A total of 1,202 male urethral swab specimens were collected in GenProbe PACE transport medium.

Steroid-induced conformational changes of rat glucocorticoid receptor cause altered trypsin cleavage of the putative helix 6 in the ligand binding domain.

Steroid-induced changes in receptor protein conformation constitute a logical means of translating the variations in steroid structures into the observed array of whole cell biological activities. One conformational change in the rat glucocorticoid receptor (GR) can be readily discerned by following the ability of trypsin digestion to afford a 16-kDa fragment. This fragment is seen after proteolysis of steroid-free receptors but disappears in digests of either glucocorticoid- or antiglucocorticoid-bound receptors.

Detection of Chlamydia trachomatis and Neisseria gonorrhoeae in swab specimens by the Hybrid Capture II and PACE 2 nucleic acid probe tests.

Background And Objectives: The Digene Hybrid Capture II (HC II) CT/GC Test (Digene Corp., Beltsville, MD) is a new nucleic acid signal amplification-based test for the detection of Chlamydia trachomatis and Neisseria gonorrhoeae in specimens from the genital tract. For optimal results, the HC II CT/GC Test employs a special conical shaped brush for cervical specimen collection from nonpregnant women and swabs from pregnant women.

Different populations of progesterone receptor-steroid complexes in binding to specific DNA sequences: effects of salts on kinetics and specificity.

We previously reported evidence for two subpopulations of several classes of steroid receptors that could be distinguished by their requirement of a low molecular weight factor (Mr=700-3000 Da) for binding to nonspecific, calf thymus DNA-cellulose [Cavanaugh, A. H. and Simons Jr.

Steroid-induced conformational changes at ends of the hormone-binding domain in the rat glucocorticoid receptor are independent of agonist versus antagonist activity.

The underlying molecular mechanism for the expression of agonist versus antagonist activity for a given receptor-steroid complex is still not known. One attractive hypothesis, based on data from progesterone receptors, is that agonist versus antagonist binding induces unique conformations at the C terminus of receptors, which can be detected by the different fragments produced by partial proteolysis. We now report that the determinants of glucocorticoid receptor (GR)-antagonist complex activity are more complex.