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Related Experiment Video

Updated: Jul 11, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Published on: January 16, 2012

Human Protein Z.

G J Broze, J P Miletich

    The Journal of Clinical Investigation
    |April 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Researchers purified Protein Z from human plasma, finding it has a short half-life during warfarin therapy. Its exact physiological function remains undetermined, despite detailed characterization.

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    Area of Science:

    • Biochemistry
    • Hematology
    • Protein Chemistry

    Background:

    • Protein Z is a protein found in human plasma.
    • Its role in coagulation or other physiological processes is not well understood.

    Purpose of the Study:

    • To purify and characterize Protein Z from human plasma.
    • To determine its concentration and half-life in patients undergoing warfarin therapy.
    • To investigate its potential enzymatic activity.

    Main Methods:

    • Protein Z purification using a four-step chromatography process.
    • Molecular weight determination and extinction coefficient calculation.
    • Plasma concentration and half-life assessment in patients on warfarin.
    • NH2-terminal sequencing and enzymatic cleavage studies.

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    Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
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    Main Results:

    • Protein Z was purified with a 20% yield.
    • It is a 62,000 mol wt protein.
    • Plasma concentration is 2.2 µg/ml, with a half-life < 2.5 days in patients starting warfarin.
    • No enzymatic activity was detected using [3H]diisopropyl fluorophosphate.

    Conclusions:

    • Protein Z has been successfully purified and characterized.
    • Its rapid clearance during warfarin therapy suggests a potential interaction with the coagulation system.
    • The physiological function of Protein Z remains unknown.