Immunochemical characterization of a low affinity lysine binding site within plasminogen

A degradation product corresponding to the fourth kringle has been isolated from porcine elastase digests of human plasminogen. An antiserum has been utilized to characterize the interaction omega -aminocarboxylic acids with a low affinity lysine binding site.

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Bibliographic Details
Published in:The Journal of biological chemistry 1981-11, Vol.256 (21), p.10864-10869
Main Authors: Plow, E F, Collen, D
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Binding, Competitive
Humans
Iodoacetates - pharmacology
Iodoacetic Acid
Kinetics
Lysine
man
Mercaptoethanol - pharmacology
omega -aminocarboxylic acids
Pancreatic Elastase
plasma
plasminogen
Plasminogen - metabolism
Protein Conformation
Swine
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Description
Summary:A degradation product corresponding to the fourth kringle has been isolated from porcine elastase digests of human plasminogen. An antiserum has been utilized to characterize the interaction omega -aminocarboxylic acids with a low affinity lysine binding site.
ISSN:0021-9258
DOI:10.1016/S0021-9258(19)68524-8