Increased awareness of event-driven PrEP and knowledge of how to use it: results from a cross-sectional survey of gay and bisexual men in Australia.

Background: Recent changes to Australian PrEP prescribing guidelines support the use of event-driven pre-exposure prophylaxis (ED-PrEP) to prevent HIV among gay and bisexual men (GBM). Social marketing campaigns to increase awareness of ED-PrEP were conducted in early 2021. This study aimed to assess the awareness and knowledge of this method after these campaigns.

Microbiology of pozol, a Mexican fermented maize dough.

Mexican fermented maize dough, pozol, including traditional banana leaf-wrapped samples and material in plastic bags, was purchased. All samples were pH 4.7 to 5.

Development of a novel substrate capture immunoassay for the detection of a neutral metalloproteinase capable of degrading basement membrane (type IV) collagen.

This paper describes the development of a modified substrate capture immunoassay useful in the detection of a neutral metalloproteinase enzyme, type IV collagenase. Capture and immobilization of this enzyme was achieved by coating the microtiter plate with gelatin, an alternative substrate for this enzyme. The captured enzyme could then be detected by affinity-purified rabbit anti-type IV collagenase antibodies prepared against synthetic peptides from the amino terminus of the enzyme.

The activation of human type IV collagenase proenzyme. Sequence identification of the major conversion product following organomercurial activation.

Type IV collagenase is a metalloproteinase which cleaves type IV collagen in a pepsin-resistant domain. Organomercurial activation of the latent 70-kDa type IV collagenase (type IV procollagenase) results in the autocatalytic removal of an amino-terminal domain resulting in the conversion to a 62-kDa activated form of the enzyme. Synthetic peptides corresponding to domains from the amino terminus (residues 1-17) and an internal domain near the carboxyl terminus (residues 472-490) were used as antigens to generate affinity-purified polyclonal antibodies which recognized their respective domains on the native type IV procollagenase.