Thrombin activity is unaltered by N-terminal truncation of factor XIII activation peptides.
Isetti, Giulia
Thrombin activity is unaltered by N-terminal truncation of factor XIII activation peptides. [electronic resource] - Biochemistry Apr 2004 - 4150-9 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi049796v doi
Amino Acid Substitution--genetics
Binding Sites--genetics
Factor XIII--chemistry
Humans
Hydrolysis
Intercellular Signaling Peptides and Proteins
Kinetics
Leucine--genetics
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments--chemical synthesis
Peptides--chemical synthesis
Protein Conformation
Protein Subunits--chemistry
Sequence Deletion
Substrate Specificity
Thrombin--metabolism
Valine--genetics
Thrombin activity is unaltered by N-terminal truncation of factor XIII activation peptides. [electronic resource] - Biochemistry Apr 2004 - 4150-9 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi049796v doi
Amino Acid Substitution--genetics
Binding Sites--genetics
Factor XIII--chemistry
Humans
Hydrolysis
Intercellular Signaling Peptides and Proteins
Kinetics
Leucine--genetics
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments--chemical synthesis
Peptides--chemical synthesis
Protein Conformation
Protein Subunits--chemistry
Sequence Deletion
Substrate Specificity
Thrombin--metabolism
Valine--genetics