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(Received for publication, May 18, 1994; and in revised form, December 12, 1994) Six glycoforms of plasminogen 2 were isolated using a
combination of lectin affinity chromatography and chromatofocussing,
and the sialic acid content of each glycoform was determined. The
kinetics of activation of each glycoform by tissue-type plasminogen
activator were analyzed on a fibrin surface and in solution. The
second-order rate constant (measured on a fibrin surface) decreased
from 1.65
Volume 270,
Number 11,
Issue of March 17, 1995 pp. 5877-5881
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
ISOLATION, CARBOHYDRATE ANALYSIS, AND KINETIC CHARACTERIZATION OF
SIX GLYCOFORMS OF PLASMINOGEN 2
10
M
s to 3.77 10
M s as the sialic
acid content of the glycoforms increased from 1.3 mol/mol of protein to
13.65 mol/mol of protein. A similar correlation was noted for
activation in solution. Each glycoform was converted to plasmin, and
the inhibition constants for the reaction between
-antiplasmin and plasmin glycoforms were determined.
All overall K
values, reflecting the final
essentially irreversible complex, were in the picomolar range. Sialic
acid does not affect inhibition of plasmin by
-antiplasmin; however, hypersialylated plasmin does
not appear to have a kringle-dependent component to inhibition.
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