Intramembrane proteases (IPs) hydrolyze peptides in the lipid membrane. IPs participate in a number of cellular pathways including immune response and surveillance, and cholesterol biosynthesis, and they are exploited by viruses for replication. Despite their broad importance across biology, how activity is regulated in the cell to control protein maturation and release of specific bioactive peptides at the right place and right time remains largely unanswered, particularly for the intramembrane aspartyl protease (IAP) subtype.
View Article and Find Full Text PDFColloids Surf B Biointerfaces
October 2022
In the present study, zinc sulfide-chitosan hybrid nanoparticles synthesized by chemical deposition were used as a matrix for the immobilization of purified α-amylase extracted from Sillago sihama (Forsskal, 1775). In this regard, the size and morphological structure of zinc sulfide-chitosan hybrid nanoparticles before and after the stabilization process were evaluated using FT-IR, DLS methods, as well as SEM and TEM electron microscopy, and EDS analyses. Then, the efficiency of the immobilized enzyme was measured in terms of temperature, optimal pH, stability at the critical temperature, and pH values.
View Article and Find Full Text PDFBackground: Ovarian reserve, vital for reproductive function, can be adversely affected by thyroid diseases. Despite alternations of thyroid hormones with ageing, data on interactions between the overtime trend of thyroid functions and ovarian reserve status has rarely been reported. We aimed to examine the overtime trend of thyroid hormones, thyroid peroxidase antibody (TPO Ab) and their associations with ovarian reserve status, identified by levels of age specific anti-mullerian hormone (AMH) in reproductive aged women, who participated in 12-year cohort of Tehran Thyroid Study (TTS).
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