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Usage Information

Structural Changes Accompanying Enzymatic Activation of Human Hageman Factor
Susan D. Revak, … , Alan R. Johnston, Tony E. Hugli
Susan D. Revak, … , Alan R. Johnston, Tony E. Hugli
Published September 1, 1974
Citation Information: J Clin Invest. 1974;54(3):619-627. https://doi.org/10.1172/JCI107799.
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Research Article

Structural Changes Accompanying Enzymatic Activation of Human Hageman Factor

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Abstract

The structure of Hageman factor, isolated from human plasma, was analyzed before and after enzymatic activation. The purified molecule is a single polypeptide chain of 80,000 molecular weight (mol wt) sedimenting at 4.5S. An amino acid analysis has been performed. The concentration of Hageman factor in normal human plasma was found to be 29 μg/ml with variation between individuals ranging from 15 to 47 μg/ml. Treatment of the molecule with kallikrein, plasmin, or trypsin resulted in cleavage at two primary sites, yielding fragments of 52,000, 40,000, and 28,000 mol wt. No further changes occurred in the fragments with subsequent reduction. Prekallikrein-activating ability was associated exclusively with the 28,000 moiety.

Authors

Susan D. Revak, Charles G. Cochrane, Alan R. Johnston, Tony E. Hugli

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Usage data is cumulative from July 2024 through July 2025.

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Text version 119 4
PDF 60 12
Scanned page 284 7
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