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Abstract
Two bovine kininogens, one with high molecular weight (HMW) and another with low molecular weight (LMW), were compared by peptide mapping, after trypsin digestion, and by polyacrylamide gel electrophoresis, after cleavage with cyanogen bromide. Almost all the fragments derived from LMW kininogen were also found in the peptide map and electropherogram of HMW kininogen. The amino acid sequence of the kallidin-containing peptide obtained from HMW kininogen was identical with that of the peptide from LMW kininogen. These results indicate a high degree of homology between the amino acid sequences of HMW and LMW kininogens.
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