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Related Concept Videos

Lipid Digestion01:06

Lipid Digestion

Lipids are large molecules that are generally not water-soluble. Since most of the digestive enzymes in the human body are water-based, there are specific steps the body must take to break down lipids and make them available for use.
Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion. The...
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...

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Related Experiment Video

Updated: Jun 19, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Lysozyme turnover in man.

N E Hansen, H Karle, V Andersen

    The Journal of Clinical Investigation
    |May 1, 1972
    PubMed
    Summary
    This summary is machine-generated.

    Plasma lysozyme turnover is rapid, influenced by kidney function and extrarenal catabolism. In kidney disease, decreased breakdown increases lysozyme levels, while in blood disorders, increased synthesis elevates levels.

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    High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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    High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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    Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
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    Published on: August 19, 2013

    A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9
    08:14

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    High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
    08:48

    High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

    Published on: April 28, 2022

    Area of Science:

    • Biochemistry
    • Nephrology
    • Hematology

    Background:

    • Plasma lysozyme plays a role in immune function.
    • Understanding lysozyme metabolism is crucial for diagnosing and managing certain diseases.

    Purpose of the Study:

    • To investigate the turnover rate and catabolism of human lysozyme in various patient groups.
    • To determine the relationship between lysozyme metabolism and renal function or hematological status.

    Main Methods:

    • Utilized (125)I-labeled human lysozyme for turnover studies.
    • Included control, nephrological (with varying renal insufficiency), and hematological patients.
    • Assessed lysozyme catabolism in relation to endogenous creatinine clearance and in anephric patients.

    Main Results:

    • Plasma lysozyme exhibits rapid turnover (fractional catabolic rate of 76%/hr).
    • Lysozyme catabolism is linked to creatinine clearance, with significant extrarenal breakdown occurring.
    • Elevated plasma lysozyme in uremia results from reduced catabolism; in hematological patients, it stems from increased synthesis.

    Conclusions:

    • Lysozyme catabolism is primarily dependent on kidney function but also occurs at extrarenal sites.
    • Plasma lysozyme levels are regulated by both synthesis and catabolism, influenced by renal and hematological conditions.
    • Findings support the hypothesis that neutrophilic granulocytes are a major source of plasma lysozyme.