Correlation of Conformation with Antibody Affinity for Fibrinogen Gamma/Chain Carboxyl Terminal Peptide Segment,

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Abstract:

The carboxyl terminal amino acids of the 411 residue fibrinogen gamma-chain play a significant role in blood clotting. One of the steps in the polymerization of fibrinogen to fibrin involves the intermolecular gamma-chain crosslinking of the side chains of Gln398 and Lys406 a process catalyzed by activated Factor XIII. The terminal portion of fibrinogen but not fibrin gamma-chain also stimulates platelet aggregation, this activity being contained within residues 400-411. Because of the physiological significance of the fibrinogen-gamma C-terminal region, antibodies have been prepared against it. We are using NMR to study the interaction of fibrinogen gamma-chain peptides with monoclonal antibody 4A5.

Author(s):
Blumenstein, Michael ; Matsueda, Gary R.
Author Organization(s):
HUNTER COLL NEW YORK
Supplementary Note:
This article is from 'Peptides. Chemistry and Biology: Proceedings of the American Peptide Symposium (12th) Held in Cambridge, Massachusetts on 16-21 June 1991', AD-A256 113, p237-238.
Pagination:
0002

Security Markings

DOCUMENT & CONTEXTUAL SUMMARY

Distribution:
Approved For Public Release

RECORD

Collection: TR
Identifying Numbers
Monitor Series:
USAMRDC
 Subject Terms
Communities of Interest:
No COI(s) Identified
Descriptor(s):
*FIBRINOGEN, *CARBOXYL RADICALS, *ANTIBODIES, BLOOD COAGULATION, NUCLEAR MAGNETIC RESONANCE, MONOCLONAL ANTIBODIES
Field(s)/Group(s):
Biochemistry
Keyword(s):
Component Reports, Binding(Biochemistry), Antibody affinity
Report Date:
1992 Jan 01