Literature DB >> 1557396

Photoaffinity labeling of the primary fibrin polymerization site: localization of the label to gamma-chain Tyr-363.

K Yamazumi1, R F Doolittle.   

Abstract

Fragment D prepared from human fibrinogen was labeled specifically by photoactivation of the peptide [14C]Gly-Pro-Arg-N-(4-azido-2-nitrophenyl)Lys amide. The preparation was freed of excess labeling reagents and then reduced and alkylated. The component alpha, beta, and gamma chains were purified by chromatography on carboxymethylcellulose and the radioactivity was found to be restricted to the gamma chain. Isolated gamma chains were digested with various endopeptidases, both alone and in tandem, and the products were fractionated by gradient HPLC. The amino acid compositions of all labeled peptides led to the conclusion that the modification occurs exclusively on gamma-chain Tyr-363.

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Year:  1992        PMID： 1557396      PMCID： PMC48769          DOI： 10.1073/pnas.89.7.2893

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  16 in total

1.  A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization.

Authors:  J Koopman; F Haverkate; E Briët; S T Lord
Journal:  J Biol Chem       Date:  1991-07-15       Impact factor: 5.157

2.  Isolation of human fibrinogen and its derivatives by affinity chromatography on Gly-Pro-Arg-Pro-Lys-Fractogel.

Authors:  C Kuyas; A Haeberli; P Walder; P W Straub
Journal:  Thromb Haemost       Date:  1990-06-28       Impact factor: 5.249

3.  Complementary DNA sequence of lamprey fibrinogen beta chain.

Authors:  V L Bohonus; R F Doolittle; M Pontes; D D Strong
Journal:  Biochemistry       Date:  1986-10-21       Impact factor: 3.162

Review 4.  Structural aspects of the fibrinogen to fibrin conversion.

Authors:  R F Doolittle
Journal:  Adv Protein Chem       Date:  1973

5.  Amino acid compositions of the subunit chains of lamprey fibrinogen. Evolutionary significance of some structural anomalies.

Authors:  R F Doolittle; B A Cottrell; M Riley
Journal:  Biochim Biophys Acta       Date:  1976-12-22

6.  Localization of a fibrin polymerization site.

Authors:  S A Olexa; A Z Budzynski
Journal:  J Biol Chem       Date:  1981-04-10       Impact factor: 5.157

7.  Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences.

Authors:  A P Laudano; R F Doolittle
Journal:  Biochemistry       Date:  1980-03-04       Impact factor: 3.162

8.  Photoaffinity labeling of the primary fibrin polymerization site: isolation and characterization of a labeled cyanogen bromide fragment corresponding to gamma-chain residues 337-379.

Authors:  A Shimizu; G M Nagel; R F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-01       Impact factor: 11.205

9.  Localization of segments essential for polymerization and for calcium binding in the gamma-chain of human fibrinogen.

Authors:  A Váradi; H A Scheraga
Journal:  Biochemistry       Date:  1986-02-11       Impact factor: 3.162

10.  Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers.

Authors:  A P Laudano; R F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  1978-07       Impact factor: 11.205
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  11 in total

1.  A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides.

Authors:  Z Yang; I Mochalkin; R F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  2000-12-19       Impact factor: 11.205

2.  Crystal structure of native chicken fibrinogen at 5.5-A resolution.

Authors:  Z Yang; I Mochalkin; L Veerapandian; M Riley; R F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  2000-04-11       Impact factor: 11.205

3.  The synthetic peptide Gly-Pro-Arg-Pro-amide limits the plasmic digestion of fibrinogen in the same fashion as calcium ion.

Authors:  K Yamazumi; R F Doolittle
Journal:  Protein Sci       Date:  1992-12       Impact factor: 6.725

4.  A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives.

Authors:  R F Doolittle
Journal:  Protein Sci       Date:  1992-12       Impact factor: 6.725

5.  Molecular analysis of scabrous mutant alleles from Drosophila melanogaster indicates a secreted protein with two functional domains.

Authors:  X Hu; E C Lee; N E Baker
Journal:  Genetics       Date:  1995-10       Impact factor: 4.562

6.  Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A alpha 20 Val --> Asp).

Authors:  S O Brennan; B Hammonds; P M George
Journal:  J Clin Invest       Date:  1995-12       Impact factor: 14.808

7.  A double-headed Gly-Pro-Arg-Pro ligand mimics the functions of the E domain of fibrin for promoting the end-to-end crosslinking of gamma chains by factor XIIIa.

Authors:  L Lorand; K N Parameswaran; S N Murthy
Journal:  Proc Natl Acad Sci U S A       Date:  1998-01-20       Impact factor: 11.205

8.  The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro.

Authors:  K P Pratt; H C Côté; D W Chung; R E Stenkamp; E W Davie
Journal:  Proc Natl Acad Sci U S A       Date:  1997-07-08       Impact factor: 11.205

9.  The minor form alpha' chain from lamprey fibrinogen is rapidly crosslinked during clotting.

Authors:  E Shipwash; Y Pan; R F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  1995-02-14       Impact factor: 11.205

10.  Photoaffinity labeling of the primary fibrin polymerization site: isolation and characterization of a labeled cyanogen bromide fragment corresponding to gamma-chain residues 337-379.

Authors:  A Shimizu; G M Nagel; R F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-01       Impact factor: 11.205
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