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Determination of the amino acid substitution in human prothrombin type 3 (157 Glu Lys) and the localization of a third thrombin cleavage site
Author(s) -
Board P. G.,
Shaw D. C.
Publication year - 1983
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1983.tb02092.x
Subject(s) - thrombin , chemistry , biochemistry , arginine , cleavage (geology) , thromboplastin , amino acid , peptide sequence , microbiology and biotechnology , biology , gene , coagulation , medicine , platelet , immunology , paleontology , fracture (geology)
S ummary . Prothrombin was purified from normal blood donors and individuals heterozygous for prothrombin type 3. Comparison of the purified prothrombin preparations by tryptic peptide mapping, amino acid analysis and automated sequencing after thrombin digestion, has indicated that prothrombin type 3 results from the substitution of a lysine residue for glutatmic acid at position 157. This substitution can result from a single base change in the structural gene and explains the relatively slow electrophoretic mobility of prothrombin type 3 at alkaline pH. An additional thrombin cleavage site in profragment 1 has been identified at arginine 54 by automated sequence analysis of thrombin digests of prothrombin.