1. Beta-Lactamase and Microbial Antibiotic Resistance

    Beta-Lactamase and Microbial Antibiotic Resistance
    β-Lactamases continue to be the leading cause of resistance to β-lactam antibiotics among gram-negative bacteria. In recent years there has been an increased incidence and prevalence of extended-spectrum β-lactamases (ESBLs), enzymes that hydrolyze and cause resistance to oxyimino-cephalosporins and aztreonam.
  2. RNase A: Frequently Asked Questions

    RNase A: Frequently Asked Questions
    Introduction to RNase Ribonucleases (RNases) are a large group of hydrolytic enzymes that degrade ribonucleic acid (RNA) molecules. These are nucleases that catalyze the breakdown of RNA into smaller components. They are a superfamily of enzymes which catalyze the degradation of RNA, operating at the levels of transcription and translation. 3D conformation of ribonuclease A enzyme These enzymes are present...
  3. Frequently Asked Questions About Proteinase K

    Frequently Asked Questions About Proteinase K
    In molecular biology Proteinase K (also protease K or endopeptidase K) is a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Engyodontium album (formerly Tritirachium album). Proteinase K is able to digest native keratin (hair), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity.
  4. Diaphorase Enzymes - What are they?

    Diaphorase Enzymes - What are they?
    Diaphorase enzymes are a class of dehydrogenase enzymes that catalyze reactions involving the nicotinamide adenine dinucleotide cofactors. Two specific members of this enzyme class, denoted as NADH diaphorase and NADPH diaphorase, are responsible for dehydrogenating the reduced forms of NAD and NADP, respectively. These enzymes, which occur naturally in all animal tissues, were first extracted in pure form by Straub...
  5. 19 X-GAL Facts and Uses You Should Know!

    X-gal is an analog of lactose, and therefore may be hydrolyzed by the β-galactosidase enzyme which cleaves the β-glycosidic bond in D-lactose.
  6. How to Use Proteases for Protein Proteolysis

    How to Use Protease/s for Protein Proteolysis Protein Proteolysis refers to the use of hydrochloric acid to destroy peptide bonds between the amino acids that make up a protein. When carried out with proteases (also known as proteinases), which are enzymes, the process is termed proteolysis. Depending on how efficient the enzyme is or what links it breaks, the proteolysis can be limited or unlimited. Proteolysis can begin either from one end of the chain of amino acids that comprise the protein or somewhere in the middle of it. Unlimited proteolysis produces individual amino acids while limited proteolysis produces short chains of polypeptides.
  7. Phosphatase Inhibitor Cocktails, Ready Made Formulations

    Invasive phosphatases can contaminate research samples and slow or halt research progress, rendering time-consuming and expensive work useless.

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