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M Pazgier

Publications and source records attributed to M Pazgier.

2 recordsLinked to original sources

Human beta-defensins.

The last decade led to the discovery and characterization of several human beta-defensins. Analysis of genomic information indicates that the number of beta-defensin-like molecules encoded by the human genome may number in the tens. Growing interest in beta-defensins steadily enhances our knowledge about various aspects of their gene location, expression patterns and the transcription factors involved in their regulation in vivo. The hallmark property of beta-defensins, their antimicrobial activity, is clearly only the tip of the iceberg in the extensive network of inter-relations within the immune system in which these peptides function. Structural studies of beta-defensins provide the molecular basis for a better understanding of their properties, functions and their potential for practical applications. In this review, we present some recent advances in the studies of human beta-defensins, with an emphasis on possible correlations between their structural and functional properties.

Amino Acid Sequence↗

Properties of cold-adapted subtilisine-like proteinase of endemic yeast Leucosporidium antarcticum.

An extracellular serine proteinase from psychrophilic marine Antarctic yeast L. antarcticum has been purified to homogeneity and characterized. The enzyme specificity, which resembles both chymotrypsin and subtilisin, as well as kinetic (topt of 25 degrees C, activity up to -20 degrees C, pHoptBzTyrOEt of 8.0-8.5), and thermodynamic properties conferring cold-adaptation of the proteinase, were determined The comparison of N-terminal sequence of 35 amino acid residues with known sequences of serine proteinases indicates that the enzyme can be preliminarly classified as a subtilisin-like proteinase, belonging to the proteinase K subfamily (clan SB, family S8, subfamily C).

Acclimatization↗