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pro vyhledávání: '"Leela Pandi"'
Autor:
Leela Pandi, Justin M. Kollman, Marcia Riley, Francisco Lopez-Lira, Russell F. Doolittle, Jason M. Burrows
Publikováno v:
Biochemistry. 48:7201-7208
When fibrin clots are formed in vitro in the presence of certain positively charged peptides, the turbidity is enhanced and fibrinolysis is delayed. Here we show that these two phenomena are not always linked and that different families of peptides b
Publikováno v:
Biochemistry. 48:3877-3886
A crystal structure of human fibrinogen has been determined at approximately 3.3 A resolution. The protein was purified from human blood plasma, first by a cold ethanol precipitation procedure and then by stepwise chromatography on DEAE-cellulose. A
Publikováno v:
Biochemistry. 45:13962-13969
The beta-chain amino-terminal sequences of all known mammalian fibrins begin with the sequence Gly-His-Arg-Pro- (GHRP-), but the homologous sequence in chicken fibrin begins with the sequence Ala-His-Arg-Pro- (AHRP-). Nonetheless, chicken fibrinogen
Autor:
Russell F. Doolittle, Leela Pandi
Publikováno v:
Biochemistry. 45:2657-2667
Synthetic peptides corresponding to the amino-terminal sequence of the beta chain of fibrin increase the turbidity of fibrin clots, whether they are generated by the direct interaction of thrombin and fibrinogen or by the reassociation of fibrin mono
Publikováno v:
Biochemistry. 41:10218-10224
The crystal structure of fragment D from lamprey fibrinogen has been determined at 2.8 A resolution. The 89 kDa protein was cocrystallized with the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens-but not lamprey-corresponds to the B knob exp
Probing the beta-chain hole of fibrinogen with synthetic peptides that differ at their amino termini
Autor:
Leela Pandi, Russell F. Doolittle
Publikováno v:
Biochemistry. 46(35)
In a recent report, we showed that alanine can replace glycine at the amino terminus of synthetic B-knobs that bind to human fibrin(ogen). We now report a survey of 13 synthetic peptides with the general sequence XHRPYam, all tested with regard to th
Publikováno v:
Biochemistry. 41(52)
The crystal structure of fragment double-D from factor XIII-cross-linked lamprey fibrin has been determined at 2.9 A resolution. The 180 kDa covalent dimer was cocrystallized with the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens, but not
Publikováno v:
Biochemistry. 40(42)
The crystal structure of native chicken fibrinogen (320 kDa) complexed with two synthetic peptides has been determined at a resolution of 2.7 A. The structure provides the first atomic-resolution view of the polypeptide chain arrangement in the centr